Information on EC 5.3.1.24 - phosphoribosylanthranilate isomerase:
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

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EC NUMBERCOMMENTARY
5.3.1.24-

RECOMMENDED NAMEGeneOntology No.
phosphoribosylanthranilate isomeraseGO:0004640

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		----
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		catalytic mechanism; kinetic mechanismEscherichia coli, Saccharomyces cerevisiae-648873
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		catalytic mechanismThermotoga maritimaQ56320648892

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Amadori rearrangementAcinetobacter calcoaceticus, Acinetobacter calcoaceticus 25001, Acinetobacter calcoaceticus 69 V, Acinetobacter calcoaceticus 69-V, Acinetobacter calcoaceticus 80-1, Acinetobacter calcoaceticus AC3, Acinetobacter calcoaceticus ADP-96, Acinetobacter calcoaceticus ATCC23055, Acinetobacter calcoaceticus BADO ADP1, Acinetobacter calcoaceticus BD 413, Acinetobacter calcoaceticus BD413, Acinetobacter calcoaceticus EBF, Acinetobacter calcoaceticus EGB, Acinetobacter calcoaceticus F45, Acinetobacter calcoaceticus F46, Acinetobacter calcoaceticus L.M.D., Acinetobacter calcoaceticus LMD 79.41, Acinetobacter calcoaceticus LMD79.41, Acinetobacter calcoaceticus MdcH, Acinetobacter calcoaceticus N.C.I.B. 8250, Acinetobacter calcoaceticus NCIM 2890, Acinetobacter calcoaceticus NCIMB 9871, Acinetobacter calcoaceticus SW1, Acinetobacter calcoaceticus ULA-501, Bacillus subtilis, [Brevibacterium] flavum, [Brevibacterium] flavum 2247, Emericella nidulans, Neurospora crassa, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Serratia marcescens 103235, Serratia marcescens 211, Serratia marcescens 2170, Serratia marcescens 2CC-1, Serratia marcescens 41002, Serratia marcescens 8000, Serratia marcescens BG, Serratia marcescens BJL200, Serratia marcescens CCTCC M 208231, Serratia marcescens CIP 6755, Serratia marcescens D 106, Serratia marcescens ECU1010, Serratia marcescens ES-2, Serratia marcescens F-1-1, Serratia marcescens HY, Serratia marcescens HY150, Serratia marcescens IAM 1022, Serratia marcescens IFO 12648, Serratia marcescens IFO3046, Serratia marcescens IFO3736, Serratia marcescens MTCC 97, Serratia marcescens NCIM 2919, Serratia marcescens SK-07, Serratia marcescens Sr41 8000, Serratia marcescens SS-1, Serratia marcescens TKU011, Serratia marcescens TPU 7303, Serratia marcescens type S, Serratia marcescens VU12944/77, Serratia marcescens W225, Serratia marcescens Ys-1, Serratia marcescens ZJB-09104--648872
Amadori rearrangementSaccharomyces cerevisiae--4611, 648870, 648873
Amadori rearrangementHansenula henricii, Hansenula henricii CCY 38-10-2--648883
Amadori rearrangementThermotoga maritima--648887, 648890, 648892
Amadori rearrangementEscherichia coli--4611, 648868, 648872, 648873, 648875, 648885, 715931
intramolecular oxidoreduction----
isomerizationStreptomyces coelicolorP16250-706633

PATHWAYKEGG LinkMetaCyc Link
Biosynthesis of secondary metabolites01110 -
Metabolic pathways01100 -
Phenylalanine, tyrosine and tryptophan biosynthesis00400 -
tryptophan biosynthesis-TRPSYN-PWY

SYSTEMATIC NAMEIUBMB Comments
N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomeraseIn some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5'-phosphoribosylanthranilate isomerase complex)----
N-(5'-phosphoribosyl)anthranilate isomeraseSaccharomyces cerevisiae--677592
N-(5'-phosphoribosyl)anthranilate isomeraseEscherichia coli--693660, 715931, 716884
N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase----
N-5’-phosphoribosylanthranilate isomerase----
PAI----
phosphoribosyl anthranilate isomeraseThermus thermophilus HB8P83825-662064
phosphoribosyl anthranilate isomeraseStreptomyces coelicolorP16250-706633
phosphoribosyl isomerase AStreptomyces coelicolorP16250-706633
phosphoribosylanthranilate isomeraseEscherichia coli--705140
PRA isomerase----
PRA isomeraseEscherichia coli--693634
PRA isomeraseStreptomyces coelicolorP16250-706633
PRAI----
PRAIEscherichia coli--693634, 705140
PRAIEscherichia coli-PRAI is the C-terminal domain of a bifunctional indole-3-glycerol phosphate synthase:N-(5'-phosphoribosyl)anthranilate isomerase enzyme in Escherichia coli715931
PRAI-LoxPEscherichia coli-variant of phosphoribosylanthranilate isomerase with an insertion coding for a Cre-lox recognition site in the loop linking alpha-helix 4 and beta-stand 5705140
PRAI[ML256-452]Escherichia coli, Saccharomyces cerevisiae-engineered monofunctional variant of IGPS:PRAI, excised monomeric domain4611, 648873
PriAStreptomyces coelicolorP16250-706633
PurF(I198V)Escherichia coli-the glutamine phosphoribosylpyrophosphate amidotransferase mutant I198V possesses detectable PRAI activity693634
Trp1pSaccharomyces cerevisiae--677592
TrpFThermotoga maritimaQ56320-648892
TrpFEscherichia coliP00909a (beta/alpha)8-barrel enzyme involved in the tryptophan biosynthetic pathway693660
TrpFEscherichia coli--716884
TtPRAIThermus thermophilus HB8P83825-662064
xPRAISaccharomyces cerevisiae-monomeric variant of PRAI from Saccharomyces cerevisiae expressed in Escherichia coli4611, 648873
isomerase, phosphoribosylanthranilate----
additional informationThermotoga maritima-imidazole glycerol phosphate synthase mutant enzyme forms that generate phosphoribosylanthranilate isomerase activity: D130V, D130T, D130P. Mutant form of EC 5.3.1.6 that generate phosphoribosylanthranilate isomerase activity: D127V, D127K, D127T, D127G, D127F, D127V/T164H662618

CAS REGISTRY NUMBERCOMMENTARY
37259-82-8-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Acinetobacter calcoaceticusnot associated with indole-3-glycerol-phosphate synthetase648872--Manually annotated by BRENDA team
Aeromonas caviaestrain ATCC 13137, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex4599--Manually annotated by BRENDA team
Arabidopsis thalianaecotype Columbia, ecotype Wassilewskija648888--Manually annotated by BRENDA team
Bacillus subtilisnot associated with indole-3-glycerol-phosphate synthetase648872--Manually annotated by BRENDA team
Bacillus subtilisnot associated with indole-3-glycerol-phosphate synthetase; strain T34593--Manually annotated by BRENDA team
Bacillus subtilis T3strain T34593--Manually annotated by BRENDA team
Citrobacter freundiistrain NCTC 6021, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex4599--Manually annotated by BRENDA team
Citrobacter freundii NCTC 6021strain NCTC 6021, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex4599--Manually annotated by BRENDA team
Coprinopsis lagopus-648869--Manually annotated by BRENDA team
Coprinopsis radiatamultifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648869--Manually annotated by BRENDA team
Emericella nidulansmultienzyme complex, in which one of the two different subunits carries three catalytic functions, including PRA isomerase and indole-3-glycerol-phosphate synthetase648872--Manually annotated by BRENDA team
Emericella nidulansmultifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648869--Manually annotated by BRENDA team
Escherichia coli-648869, 716884--Manually annotated by BRENDA team
Escherichia coli-705140, 715931P00909UniProtManually annotated by BRENDA team
Escherichia colibifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex4611, 638666, 648868, 648873, 648876, 648885--Manually annotated by BRENDA team
Escherichia colibifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex; strain W3110648872, 648875--Manually annotated by BRENDA team
Escherichia colistrain K-12693634--Manually annotated by BRENDA team
Escherichia colistrain M15693660P00909UniProtManually annotated by BRENDA team
Escherichia coli W3110strain W3110648872, 648875--Manually annotated by BRENDA team
Haloferax volcanii-648880--Manually annotated by BRENDA team
Hansenula henriciistrain CCY 38-10-2, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648883--Manually annotated by BRENDA team
Hansenula henricii CCY 38-10-2strain CCY 38-10-2, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648883--Manually annotated by BRENDA team
Metarhizium anisopliae-661544Q873X5UniprotManually annotated by BRENDA team
Neurospora crassaa fragment of the beta subunit of the multifunctional alpha2beta2 anthranilate synthetase complex has PRA isomerase and indole-3-glycerol phosphate synthetase activities, organization of the functional domains of the compex648877--Manually annotated by BRENDA team
Neurospora crassacomponent IIb of the anthranilate synthetase complex with PRA isomerase and indole-3-glycerol phosphate synthetase activities; multienzyme complex, in which one of the two different subunits carries three catalytic functions, including PRA isomerase and indole-3-glycerol-phosphate synthetase648874--Manually annotated by BRENDA team
Neurospora crassamultienzyme complex, in which one of the two different subunits carries three catalytic functions, including PRA isomerase and indole-3-glycerol-phosphate synthetase648872--Manually annotated by BRENDA team
Neurospora crassamultifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648869--Manually annotated by BRENDA team
Pectobacterium carotovorumstrain ICPB EC153, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex4599--Manually annotated by BRENDA team
Pectobacterium carotovorum ICPB EC153strain ICPB EC153, bifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex4599--Manually annotated by BRENDA team
Phytophthora parasiticabifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648879P24920SwissProtManually annotated by BRENDA team
Pisum sativum-648871--Manually annotated by BRENDA team
Proteus vulgarisbifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex4599--Manually annotated by BRENDA team
Pseudomonas putidanot associated with indole-3-glycerol-phosphate synthetase648872--Manually annotated by BRENDA team
Saccharomyces cerevisiae-677592--Manually annotated by BRENDA team
Saccharomyces cerevisiaenaturally monofunctional enzyme638666--Manually annotated by BRENDA team
Saccharomyces cerevisiaenaturally monofunctional enzyme; xPRAI648873--Manually annotated by BRENDA team
Saccharomyces cerevisiaeseparate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase648869--Manually annotated by BRENDA team
Saccharomyces cerevisiaeseparate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase; transformant strain RH218 (YARp1)648870--Manually annotated by BRENDA team
Saccharomyces cerevisiaexPRAI4611--Manually annotated by BRENDA team
Saccharomyces cerevisiae xPRAIxPRAI4611, 648873--Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimuriummultifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648872--Manually annotated by BRENDA team
Schizosaccharomyces pombemultifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648869--Manually annotated by BRENDA team
Serratia marcescensbifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex648872--Manually annotated by BRENDA team
Serratia marcescensbifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex; strain HY4601--Manually annotated by BRENDA team
Serratia marcescens HYstrain HY4601--Manually annotated by BRENDA team
Serratia rubidaeabifunctional indole-3-glycerol-phosphate synthetase/PRA isomerase complex4599--Manually annotated by BRENDA team
Streptomyces coelicolor-660613--Manually annotated by BRENDA team
Streptomyces coelicolor-706633P16250UniProtManually annotated by BRENDA team
Thermotoga maritimaimidazole glycerol phosphate synthase mutant enzyme forms that generate phosphoribosylanthranilate isomerase activity: D130V, D130T, D130P. Mutant form of EC 5.3.1.6 that generate phosphoribosylanthranilate isomerase activity: D127V, D127K, D127T, D127G, D127F, D127V/T164H662618--Manually annotated by BRENDA team
Thermotoga maritimamonofunctional enzyme648886, 648887, 648890--Manually annotated by BRENDA team
Thermotoga maritimamonofunctional enzyme648892Q56320UniprotManually annotated by BRENDA team
Thermotoga maritimamonofunctional enzyme; Protein Data Bank: 1NSJ648889Q56320UniprotManually annotated by BRENDA team
Thermus thermophilus HB8-662064P83825UniprotManually annotated by BRENDA team
Zea mays-648871--Manually annotated by BRENDA team
[Brevibacterium] flavumindole-3-glycerol-phosphate synthetase and PRA isomerase form an easily dissociable multienzyme complex648872--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismStreptomyces coelicolorP16250phosphoribosyl isomerase A takes part in histidine and tryptophan biosynthesis706633

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium--648872-648872ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Bacillus subtilis--4593-4593?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Bacillus subtilis--648872-648872ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli--4611-4611?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli--638666-638666?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli--648868-648868?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli--648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli--648875-648875?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli--648885-648885?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli--693634--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coliP00909-693660--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae--4611-4611?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae--638666-638666?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae--648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae--648870-648870ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Emericella nidulans--648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Emericella nidulans--648872-648872ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Neurospora crassa--648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Neurospora crassa--648874-648874?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Neurospora crassa--648877-648877?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Neurospora crassa--648872-648872ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Pisum sativum, Zea mays--648871-648871?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Arabidopsis thaliana--648888-648888?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Pseudomonas putida, Acinetobacter calcoaceticus--648872-648872ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Haloferax volcanii--648880-648880?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Serratia marcescens--4601-4601?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Serratia marcescens--648872-648872ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Proteus vulgaris--4599-4599?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Schizosaccharomyces pombe--648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		[Brevibacterium] flavum--648872-648872ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Aeromonas caviae, Pectobacterium carotovorum, Citrobacter freundii, Serratia rubidaea--4599-4599?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Hansenula henricii--648883-648883?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima--648890-648890ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Coprinopsis lagopus, Coprinopsis radiata--648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Phytophthora parasiticaP24920-648879-648879?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Streptomyces coelicolorP16250-706633--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli--715931--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli, Saccharomyces cerevisiae-mechanism648873enolamine is the first product, which then tautomerizes to the alpha-amino ketone648873r
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-enzyme structure648886-648886?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritimaQ56320enzyme structure648889-648889?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-structure of the indole-3-glycerol-phosphate synthetase/PRA isomerase complex, 2 well-defined functional domains: N-terminal indole-3-glycerol-phosphate synthetase, residues 1-255, and C-terminal PRA isomerase, residues 256-452, with limited noncovalent contacts between the domains, the two reactions are catalyzed independently from each other648876-648876?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-structure of the indole-3-glycerol-phosphate synthetase/PRA isomerase complex, 2 well-defined functional domains: N-terminal indole-3-glycerol-phosphate synthetase, residues 1-255, and C-terminal PRA isomerase, residues 256-452, with limited noncovalent contacts between the domains, the two reactions are catalyzed independently from each other648872-648872ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-thermodynamic equilibrium strongly favors the product648873enolamine is the first product, which then tautomerizes to the alpha-amino ketone648873r
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritimaQ56320high catalytic efficiency648889-648889?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritimaQ56320high catalytic efficiency648892-648892?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-high catalytic efficiency648887-648887ir
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritimaQ56320reaction mechanism involving general acid-base catalysis and a Schiff base intermediate, Cys-7 and Asp-126 are important for the reaction648892-648892?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium, Bacillus subtilis, Escherichia coli, Emericella nidulans, Neurospora crassa, Pseudomonas putida, Acinetobacter calcoaceticus, Serratia marcescens, [Brevibacterium] flavum-fourth step in tryptophan biosynthesis648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-fourth step in tryptophan biosynthesis648886-648886?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-fourth step in tryptophan biosynthesis648887-648887?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-fourth step in tryptophan biosynthesis648890-648890?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-third step in tryptophan biosynthesis648868-648868?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-third step in tryptophan biosynthesis648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-third step in tryptophan biosynthesis648873-648873?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-third step in tryptophan biosynthesis648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-third step in tryptophan biosynthesis648870-648870?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-third step in tryptophan biosynthesis648873-648873?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Emericella nidulans, Neurospora crassa, Schizosaccharomyces pombe, Coprinopsis lagopus, Coprinopsis radiata-third step in tryptophan biosynthesis648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium-involved in tryptophan biosynthesis from chorismate648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Bacillus subtilis-involved in tryptophan biosynthesis from chorismate4593--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Bacillus subtilis-involved in tryptophan biosynthesis from chorismate648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate4611-4611?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate638666-638666?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648868-648868?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648873-648873?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648875-648875?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648876-648876?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648885-648885?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate4611-4611?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate638666-638666?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate648870-648870?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate648873-648873?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Emericella nidulans-involved in tryptophan biosynthesis from chorismate648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Emericella nidulans-involved in tryptophan biosynthesis from chorismate648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Neurospora crassa-involved in tryptophan biosynthesis from chorismate648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Neurospora crassa-involved in tryptophan biosynthesis from chorismate648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Arabidopsis thaliana-involved in tryptophan biosynthesis from chorismate648888--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Pseudomonas putida, Acinetobacter calcoaceticus-involved in tryptophan biosynthesis from chorismate648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Haloferax volcanii-involved in tryptophan biosynthesis from chorismate648880--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Serratia marcescens-involved in tryptophan biosynthesis from chorismate4601--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Serratia marcescens-involved in tryptophan biosynthesis from chorismate648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Proteus vulgaris-involved in tryptophan biosynthesis from chorismate4599-4599?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Schizosaccharomyces pombe-involved in tryptophan biosynthesis from chorismate648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		[Brevibacterium] flavum-involved in tryptophan biosynthesis from chorismate648872-648872?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Aeromonas caviae, Pectobacterium carotovorum, Citrobacter freundii, Serratia rubidaea-involved in tryptophan biosynthesis from chorismate4599-4599?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Hansenula henricii-involved in tryptophan biosynthesis from chorismate648883-648883?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-involved in tryptophan biosynthesis from chorismate648887-648887?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritimaQ56320involved in tryptophan biosynthesis from chorismate648892-648892?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Coprinopsis lagopus, Coprinopsis radiata-involved in tryptophan biosynthesis from chorismate648869-648869?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Phytophthora parasiticaP24920involved in tryptophan biosynthesis from chorismate648879--?
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-imidazole glycerol phosphate synthase mutant enzyme forms that generate phosphoribosylanthranilate isomerase activity: D130V, D130T, D130P. Mutant form of EC 5.3.1.6 that generate phosphoribosylanthranilate isomerase activity: D127V, D127K, D127T, D127G, D127F, D127V/T164H662618--?
additional information?-Saccharomyces cerevisiae-the enzyme is essential for cell proliferation in the absence of tryptophan677592---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Streptomyces coelicolorP16250-706633--
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium, Bacillus subtilis, Escherichia coli, Emericella nidulans, Neurospora crassa, Pseudomonas putida, Acinetobacter calcoaceticus, Serratia marcescens, [Brevibacterium] flavum-fourth step in tryptophan biosynthesis648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-fourth step in tryptophan biosynthesis648886-648886
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-fourth step in tryptophan biosynthesis648887-648887
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-fourth step in tryptophan biosynthesis648890-648890
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-third step in tryptophan biosynthesis648868-648868
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-third step in tryptophan biosynthesis648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-third step in tryptophan biosynthesis648873-648873
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-third step in tryptophan biosynthesis648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-third step in tryptophan biosynthesis648870-648870
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-third step in tryptophan biosynthesis648873-648873
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Emericella nidulans, Neurospora crassa, Schizosaccharomyces pombe, Coprinopsis lagopus, Coprinopsis radiata-third step in tryptophan biosynthesis648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Salmonella enterica subsp. enterica serovar Typhimurium-involved in tryptophan biosynthesis from chorismate648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Bacillus subtilis-involved in tryptophan biosynthesis from chorismate4593--
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Bacillus subtilis-involved in tryptophan biosynthesis from chorismate648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate4611-4611
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate638666-638666
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648868-648868
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648873-648873
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648875-648875
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648876-648876
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Escherichia coli-involved in tryptophan biosynthesis from chorismate648885-648885
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate4611-4611
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate638666-638666
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate648870-648870
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Saccharomyces cerevisiae-involved in tryptophan biosynthesis from chorismate648873-648873
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Emericella nidulans-involved in tryptophan biosynthesis from chorismate648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Emericella nidulans-involved in tryptophan biosynthesis from chorismate648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Neurospora crassa-involved in tryptophan biosynthesis from chorismate648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Neurospora crassa-involved in tryptophan biosynthesis from chorismate648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Arabidopsis thaliana-involved in tryptophan biosynthesis from chorismate648888--
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Pseudomonas putida, Acinetobacter calcoaceticus-involved in tryptophan biosynthesis from chorismate648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Haloferax volcanii-involved in tryptophan biosynthesis from chorismate648880--
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Serratia marcescens-involved in tryptophan biosynthesis from chorismate4601--
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Serratia marcescens-involved in tryptophan biosynthesis from chorismate648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Proteus vulgaris-involved in tryptophan biosynthesis from chorismate4599-4599
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Schizosaccharomyces pombe-involved in tryptophan biosynthesis from chorismate648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		[Brevibacterium] flavum-involved in tryptophan biosynthesis from chorismate648872-648872
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Aeromonas caviae, Pectobacterium carotovorum, Citrobacter freundii, Serratia rubidaea-involved in tryptophan biosynthesis from chorismate4599-4599
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Hansenula henricii-involved in tryptophan biosynthesis from chorismate648883-648883
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritima-involved in tryptophan biosynthesis from chorismate648887-648887
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Thermotoga maritimaQ56320involved in tryptophan biosynthesis from chorismate648892-648892
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Coprinopsis lagopus, Coprinopsis radiata-involved in tryptophan biosynthesis from chorismate648869-648869
N-(5-phospho-beta-D-ribosyl)anthranilate1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
show the reaction diagram		Phytophthora parasiticaP24920involved in tryptophan biosynthesis from chorismate648879--
additional information?-Saccharomyces cerevisiae-the enzyme is essential for cell proliferation in the absence of tryptophan677592--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateEscherichia coli-product inhibition4611 2D-image
CoCl2Hansenula henricii-0.001 mM, 20% inhibition648883 2D-image
CuSO4Hansenula henricii-0.001 mM, 100% inhibition648883 2D-image
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateAcinetobacter calcoaceticus, Bacillus subtilis, [Brevibacterium] flavum, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens--648872-
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateEscherichia coli, Saccharomyces cerevisiae-competitive inhibitor4611, 648873-
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateEscherichia coli--648872, 648876-
Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateThermotoga maritima-binds reversibly; competitive inhibitor648887-
MnCl2Hansenula henricii-0.001 mM, 45% inhibition648883 2D-image
additional informationEscherichia coli-not inhibited by indoleglycerol phosphate4611-
additional informationEscherichia coli-chemically synthesized N-(5-phospho-beta-D-ribosyl)anthranilate contains inhibitors, but not if it is generated by anthranilate phosphoribosyltransferase638666-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00028-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, dimer648886, 648887 2D-image
0.00028-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritimaQ56320pH 7.5, 25°C, dimer648889 2D-image
0.00028-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, dimer648890 2D-image
0.00028-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritimaQ56320pH 7.5, 25°C, dimer648892 2D-image
0.00039-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 45°C, dimer648887, 648890 2D-image
0.00073-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 60°C, dimer648887, 648890 2D-image
0.00103-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 80°C, dimer648887, 648890 2D-image
0.0032-N-(5-phospho-beta-D-ribosyl)anthranilateSaccharomyces cerevisiae-pH 7.5, 25°C, recombinant xPRAI, expressed in Escherichia coli648873 2D-image
0.0040.005N-(5-phospho-beta-D-ribosyl)anthranilateSaccharomyces cerevisiae-30°C648870 2D-image
0.004-N-(5-phospho-beta-D-ribosyl)anthranilateStreptomyces coelicolorP16250PriA, PRA isomerase activity706633 2D-image
0.0047-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-25°C, monomeric domain PRAI[ML256-452]4611 2D-image
0.0047-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-25°C, monomeric domain PRAI[ML256-452]; pH 7.5648873 2D-image
0.0049-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-25°C, bifunctional IGPS:PRAI4611 2D-image
0.0049-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-25°C, bifunctional IGPS:PRAI; pH 7.5638666 2D-image
0.0049-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli--648868 2D-image
0.0049-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-25°C, bifunctional IGPS:PRAI; pH 7.5648873 2D-image
0.005-N-(5-phospho-beta-D-ribosyl)anthranilateStreptomyces coelicolorP16250PriA, PRA isomerase activity706633 2D-image
0.007-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-pH 7.5, 20°C648872 2D-image
0.0083-N-(5-phospho-beta-D-ribosyl)anthranilateStreptomyces coelicolorP16250PriA mutant R19A, PRA isomerase activity706633 2D-image
0.026-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127G, mutant form of EC 5.3.1.6662618 2D-image
0.03-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127K, mutant form of EC 5.3.1.6662618 2D-image
0.04-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D130P, mutant form of imidazole glycerol phosphate synthase662618 2D-image
0.041-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127F, mutant form of EC 5.3.1.6662618 2D-image
0.043-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127T, mutant form of EC 5.3.1.6662618 2D-image
0.045-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D130T, mutant form of imidazole glycerol phosphate synthase662618 2D-image
0.051-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127V/T164H, mutant form of EC 5.3.1.6662618 2D-image
0.074-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127V, mutant form of EC 5.3.1.6; pH 7.5, 25°C, D130V, mutant form of imidazole glycerol phosphate synthase662618 2D-image
1.3-N-(5-phospho-beta-D-ribosyl)anthranilateHansenula henricii-pH 7.6648883 2D-image
additional information-additional informationEscherichia coli-increasing the pH from 7.5 to 8.6 increases the Km638666-
additional information-additional informationEscherichia coli--648875-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.000092-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D130T, mutant form of imidazole glycerol phosphate synthase662618 2D-image
0.00018-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D130V, mutant form of imidazole glycerol phosphate synthase662618 2D-image
0.00022-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D130P, mutant form of imidazole glycerol phosphate synthase662618 2D-image
0.0013-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127G, mutant form of EC 5.3.1.6662618 2D-image
0.0017-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127K, mutant form of EC 5.3.1.6662618 2D-image
0.0023-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127F, mutant form of EC 5.3.1.6662618 2D-image
0.0027-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127T, mutant form of EC 5.3.1.6662618 2D-image
0.0086-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127V, mutant form of EC 5.3.1.6662618 2D-image
0.009-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, D127V/T164H, mutant form of EC 5.3.1.6662618 2D-image
1.4-N-(5-phospho-beta-D-ribosyl)anthranilateStreptomyces coelicolorP16250PriA mutant R19A, PRA isomerase activity706633 2D-image
3.4-N-(5-phospho-beta-D-ribosyl)anthranilateStreptomyces coelicolorP16250PriA, PRA isomerase activity706633 2D-image
3.7-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 25°C, dimer648886, 648887, 648890 2D-image
3.7-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritimaQ56320pH 7.5, 25°C, dimer648892 2D-image
12-N-(5-phospho-beta-D-ribosyl)anthranilateStreptomyces coelicolorP16250PriA, PRA isomerase activity706633 2D-image
13.5-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 45°C, dimer648887, 648890 2D-image
32-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-25°C, monomeric domain PRAI[ML256-452]4611 2D-image
32-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-25°C, monomeric domain PRAI[ML256-452]; pH 7.5648873 2D-image
38.5-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 60°C, dimer648887, 648890 2D-image
39-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-pH 7.5, 20°C648872 2D-image
40-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-25°C; bifunctional IGPS:PRAI4611 2D-image
40-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-bifunctional IGPS:PRAI638666 2D-image
40-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli-bifunctional IGPS:PRAI; pH 7.5, 25°C648873 2D-image
5060N-(5-phospho-beta-D-ribosyl)anthranilateSaccharomyces cerevisiae-30°C648870 2D-image
50-N-(5-phospho-beta-D-ribosyl)anthranilateEscherichia coli--648868 2D-image
69-N-(5-phospho-beta-D-ribosyl)anthranilateSaccharomyces cerevisiae-pH 7.5, 25°C, recombinant xPRAI, expressed in E. coli648873 2D-image
130-N-(5-phospho-beta-D-ribosyl)anthranilateThermotoga maritima-pH 7.5, 80°C, dimer648887, 648890 2D-image
additional information-additional informationThermotoga maritima-values for PRAI variants648886-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0017-Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateSaccharomyces cerevisiae-pH 7.5, 25°C, recombinant xPRAI, expressed in Escherichia coli648873-
0.0022-Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateSaccharomyces cerevisiae-recombinant xPRAI, expressed in Escherichia coli4611-
0.0065-Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateEscherichia coli-25°C, bifunctional IGPS:PRAI4611-
0.0065-Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateEscherichia coli-25°C, bifunctional IGPS:PRAI; pH 7.5648873-
0.0068-Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateEscherichia coli-25°C, monomeric domain PRAI[ML256-452]4611-
0.0068-Reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateEscherichia coli-25°C, monomeric domain PRAI[ML256-452]; pH 7.5648873-

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.0071-Hansenula henricii CCY 38-10-2, Hansenula henricii-pH 7.6648883
5.15-Bacillus subtilis--4593
5.5-Serratia marcescens-37°C, indole-3-glycerol-phosphate synthetase/PRA isomerase complex4601
8.78-Escherichia coli-37°C648872
14.3-Thermotoga maritima-37°C648890
98.7-Escherichia coli-monofunctional domain PRAI[ML256-452]4611
102-Saccharomyces cerevisiae--648870
additional information-Saccharomyces cerevisiae--648870
additional information-Thermotoga maritima-values for PRAI variants648886
additional information-Thermotoga maritima--648887
additional information-Saccharomyces cerevisiae--677592

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.5-Escherichia coli, Saccharomyces cerevisiae-assay at638666
7.5-Thermotoga maritima-assay at648886, 648887
7.5-Thermotoga maritimaQ56320assay at648892
7.5-Streptomyces coelicolorP16250activity assay706633
7.6-Hansenula henricii--648883
8.6-Escherichia coli-assay at648872

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Escherichia coli, Saccharomyces cerevisiae-assay at638666
25-Escherichia coli, Saccharomyces cerevisiae-assay at648873
25-Thermotoga maritima-assay at648886, 648887
25-Thermotoga maritimaQ56320assay at648892
25-Streptomyces coelicolorP16250activity assay706633
37-Serratia marcescens-assay at4601
37-Neurospora crassa-assay at648874

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
myceliumNeurospora crassa--648877Manually annotated by BRENDA team
seedlingArabidopsis thaliana-transgenic, ecotype Columbia648888Manually annotated by BRENDA team
additional informationArabidopsis thaliana-ecotype Columbia, expression patterns of the 3 PAI isogenes, which are differentially regulated under normal growth conditions and differentially expressed in a tissue- and cell-type-specific manner648888Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
2kzh, downloadSCOP (2kzh)CATH (2kzh)Escherichia coli (strain K12)
2y85, downloadSCOP (2y85)CATH (2y85)Mycobacterium tuberculosis
2y88, downloadSCOP (2y88)CATH (2y88)Mycobacterium tuberculosis
2y89, downloadSCOP (2y89)CATH (2y89)Mycobacterium tuberculosis
3zs4, downloadSCOP (3zs4)CATH (3zs4)Mycobacterium tuberculosis
4aaj, downloadSCOP (4aaj)CATH (4aaj)Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
1vzw, downloadSCOP (1vzw)CATH (1vzw)Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
2vep, downloadSCOP (2vep)CATH (2vep)Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
2x30, downloadSCOP (2x30)CATH (2x30)Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
1dl3, downloadSCOP (1dl3)CATH (1dl3)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
1lbm, downloadSCOP (1lbm)CATH (1lbm)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
1nsj, downloadSCOP (1nsj)CATH (1nsj)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
1v5x, downloadSCOP (1v5x)CATH (1v5x)Thermus thermophilus

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
22900-Escherichia coli-PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 2.0 microM; PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 20 microM705140
23000-Escherichia coli-monomeric domain PRAI[ML256-452], gel filtration and analytical ultracentrifugation4611
23000-Saccharomyces cerevisiae--4611
23000-Saccharomyces cerevisiae-gel filtration648870
23100-Escherichia coliP00909calculated from amino acid sequence693660
24100-Escherichia coli-PRAI-LoxP, theoretical705140
26300-Bacillus subtilis-gel filtration4593
30200-Thermotoga maritima-dimer, gel filtration648886, 648890
45000-Aeromonas caviae, Serratia rubidaea-indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration4599
46000-Escherichia coli-indole-3-glycerol-phosphate synthetase/PRA isomerase complex, sedimentation equilibrium648875
47000-Citrobacter freundii-indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration4599
48000-Pectobacterium carotovorum-indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration4599
48000-Serratia marcescens-indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration4601
49600-Thermotoga maritima-dimer, sedimentation equilibrium analysis648886, 648887, 648890
49800-Escherichia coli-PRAI-LoxP, His-tag, apparent molecular mass, protein concentration 100 microM, deduced association state dimer705140
53000-Proteus vulgaris-indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration4599
56000-Neurospora crassa-indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit, gel filtration648877
160000-Neurospora crassa-component IIb of the anthranilate synthetase complex with PRA isomerase and indole-3-glycerol phosphate synthetase activities, gel filtration648874
185000-Hansenula henricii-indole-3-glycerol-phosphate synthetase/PRA isomerase complex, gel filtration648883
additional information-Thermotoga maritima-MWs of PRAI variants648886

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerNeurospora crassa-active form648869
dimerNeurospora crassa-the indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunit exists as a dimer648877
dimerThermotoga maritimaQ56320-648892
dimerThermus thermophilus HB8P83825-662064
dimerEscherichia coliP00909-693660
homodimerThermotoga maritima-2 * 23040, calculated from the amino acid sequence; 2 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop648886
homodimerThermotoga maritimaQ563202 identical (betaalpha)8-barrel subunits, which are associated back-to-back and locked together by a hydrophobic loop648889
homodimerThermotoga maritima-2 * 23040, calculated from the amino acid sequence648887, 648890
monomerBacillus subtilis-1 * 21800, SDS-PAGE4593
monomerSerratia marcescens-1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE4601
monomerSaccharomyces cerevisiae--648870
monomerAcinetobacter calcoaceticus, Bacillus subtilis-separate monomeric enzyme648872
monomerEscherichia coli-1 * 49370, calculated from the amino acid sequence; 1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex648872
monomerPseudomonas putida-separate monomeric enzyme648872
monomerSalmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens-1 * 49400, indole-3-glycerol-phosphate synthetase/PRA isomerase complex648872
monomerEscherichia coli-1 * 48000, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, SDS-PAGE648875
monomerEscherichia coli-1 * 49500, indole-3-glycerol-phosphate synthetase/PRA isomerase complex, amino acid sequence analysis648885
monomerEscherichia coli--648876, 705140
monomerEscherichia coli-1 * 15100, multi-angle laser light-scattering715931
monomerEscherichia coli-x-ray crystallography716884

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coli-4611, 648872, 648875
repeated seeding technique; three-dimensional structure of indole-3-glycerol-phosphate synthetase/PRA isomerase complex determined by X-ray crystallographyEscherichia coli-648885
three-dimensional structure of indole-3-glycerol-phosphate synthetase/PRA isomerase complex determined by X-ray crystallographyEscherichia coli-648876
hanging-drop vapour-diffusion method, crystallized using the hanging-drop method in 1.5 M ammonium sulfate and 100 mM sodium citrate pH 4.8. Crystals are obtained up to 0.05 * 0.05 * 0.3 mM size, space group P3(1,2)21, unit cell parameters a = 65.1 A, c = 104.7 AStreptomyces coelicolor-660613
the structure of the PriA mutant R139N is determined to a resolution of 1.95 AStreptomyces coelicolorP16250706633
hanging drop vapor diffusion methodThermotoga maritima-648887
hanging drop vapor diffusion method; X-ray structure of a complex between TrpF and its product analogue reduced 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphateThermotoga maritimaQ56320648892
mutationally generated monomeric PRA isomerase, comparison to PRAI dimerThermotoga maritima-648886
x-ray structureThermotoga maritima-648889, 648890
oil microbatch methodThermus thermophilus HB8P83825662064

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
3.2-Thermotoga maritima-strongly resistant toward inactivation by acidification to pH 3.2648887
6.57.5Escherichia coli-25°C, 16 h, most stable in potassium phosphate buffer, in presence of 1 mM dithioerythritol648875
additional information-Thermotoga maritima-extremely stable towards acidic pH648886
additional information-Thermus thermophilus HB8P83825denaturation at acidic pH is correlated with the dissociation of its dimeric form662064

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4850Escherichia coliP00909the melting temperatures of wild type TrpF are 48 and 50°C when the protein concentrations are 0.002 and 0.02 mM, respectively693660
85-Thermotoga maritima-dimer, half-life: 310 min; monomeric variants, half-life: 3-5 min648886
85-Thermotoga maritima-dimer, half-life: 310 min648887, 648890
91.5-Thermotoga maritima-dimer, half-life: 50 min648887
95-Thermotoga maritima-dimer, strongly resistant toward inactivation up to 95°C, half-life: 21 min648887
additional information-Thermotoga maritima-extremely thermostable; mutationally generated monomers of PRAI are as active as the dimer, but far more thermolabile648886
additional information-Thermotoga maritimaQ56320structural features resonsible for the high thermostability648889
additional information-Thermotoga maritima-structural features resonsible for the high thermostability648890
additional information-Thermotoga maritimaQ56320extremely thermostable648892

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
10-15% v/v glycerol stabilizesBacillus subtilis-4593
enzyme is resistant to protease attackEscherichia coli-648872
extremely stable enzymeThermotoga maritima-648886, 648887, 648890
extremely stable towards proteolytic attackThermotoga maritima-648886, 648887

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
very susceptible to autooxidation catalyzed by Cu2+ and other heavy metal ions, oxidation is prevented by EDTA and dithioerythritolEscherichia coli-648872

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, 0.8 M sucrose, 7 days, 20% loss of activity, 15 days, 65% loss of activityBacillus subtilis-4593
4°C, 10-15% v/v glycerol, 6-15 days, average of 24% loss of activityBacillus subtilis-4593
4°C, under argon, months, stableEscherichia coli-648872
4°C, 24h, 35% loss of activityHansenula henricii, Hansenula henricii CCY 38-10-2-648883

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bacillus subtilis-4593
a nickel Sepharose column, HisTrap FF, and a gel-filtration column, Sephacryl S200, are usedEscherichia coli-705140
best isolated from mutant trp A2; indole-3-glycerol-phosphate synthetase/PRA isomerase complexEscherichia coli-648868
HisTrap FF nickel affinity column chromatographyEscherichia coli-716884
indole-3-glycerol-phosphate synthetase/PRA isomerase complexEscherichia coli-638666, 648872, 648875, 648885
monomeric domain PRAI[ML256-452] and bifunctional IGPS:PRAIEscherichia coli-4611, 648873
Ni-NTA agarose column chromatography and Superdex 75 gel filtrationEscherichia coli-715931
Ni-NTA column chromatographyEscherichia coli-693634
Ni-NTA column chromatography, HiTrap Q column chromatography, Superdex 200 gel filtrationEscherichia coliP00909693660
21foldHansenula henricii, Hansenula henricii CCY 38-10-2-648883
component IIb of the anthranilate synthetase complex, purified from trp2 mutantNeurospora crassa-648874
indole-3-glycerol-phosphate synthetase/PRA isomerase fragment of the multifunctional anthranilate synthetase complex beta subunitNeurospora crassa-648877
partialPisum sativum-648871
-Saccharomyces cerevisiae-638666
165foldSaccharomyces cerevisiae-648870
recombinant xPRAI, expressed in Escherichia coliSaccharomyces cerevisiae-4611, 648873
indole-3-glycerol-phosphate synthetase/PRA isomerase complex, 70foldSerratia marcescens-4601
-Streptomyces coelicolor-660613, 706633
mutationally generated monomeric PRA isomeraseThermotoga maritima-648886
recombinant PRAI, expressed in Escherichia coliThermotoga maritima-648887, 648890
TrpF mutants C7A, D126N and C7A/D126N double mutantThermotoga maritimaQ56320648892
-Thermus thermophilus HB8P83825662064
partialZea mays-648871

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
ecotype Columbia, 3 PAI isogenes: PAI1, PAI2 and PAI3Arabidopsis thaliana-648888
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesisCoprinopsis lagopus-648869
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis; TRPC gene encoding multifunctional enzyme is cloned in Escherichia coli and sequencedEmericella nidulans-648869
expressed in Escherichia coli BL21(DE3) cellsEscherichia coli-715931
expressed in Escherichia coli M15 (pREP4) cellsEscherichia coli-716884
expressed in Escherichia coli XL1-Red cellsEscherichia coli-693634
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesisEscherichia coli-648869
separation of the 2 domains of the indole-3-glycerol-phosphate synthetase/PRA isomerase complex on the gene level, expression of monofunctional PRAI[ML256-452] in Escherichia coli W3110 trpR, deltatrp EA2Escherichia coli-4611
sequence of trpCF gene encoding indole-3-glycerol-phosphate synthetase/PRA isomerase complexEscherichia coli-648876
the expression of PRAI-LoxP variants is performed in Escherichia coli Rosetta 2 cells transformed with pET28b+ plasmids containing the encoding sequencesEscherichia coli-705140
trpDFEG gene cluster, trpF gene encodes PRA isomeraseHaloferax volcanii-648880
-Metarhizium anisopliaeQ873X5661544
-Metarhizium anisopliae CQMa102-661544
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis; TRP1 gene encoding multifunctional enzyme is cloned in Escherichia coli and sequencedNeurospora crassa-648869
TRP1 gene encoding indole-3-glycerol-phosphate synthetase/PRA isomerase complex is cloned, expressed in Escherichia coli and sequencedPhytophthora parasiticaP24920648879
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesis; separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase; TRP1 gene is cloned in Escherichia coli and sequencedSaccharomyces cerevisiae-648869
separate enzyme encoded by an independent gene, not associated with indole-3-glycerol-phosphate synthetase; TRP1 gene regulation, cloningSaccharomyces cerevisiae-648870
overview over trp/TRP genes encoding PRAI, functional organization of enzymes of tryptophan biosynthesisSchizosaccharomyces pombe-648869
-Streptomyces coelicolor-660613
into the vector pET-15bStreptomyces coelicolorP16250706633
cloning of trpF mutants, expression in Escherichia coli BL21(DE3)Thermotoga maritima-648886, 648892
trpF gene is cloned and expressed in Escherichia coliThermotoga maritima-648887, 648889, 648890

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Mut_L2_FBPAEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 2, sequence of loop SNGGASFIAGKGVKSDVPQ, fructose-bisphosphate aldolase, EC 4.1.2.13705140
Mut_L2_MREscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 2, sequence of loop GYPAL, mandelate racemase, EC 5.1.2.2705140
Mut_L2_PRAI_WTEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 2, sequence of loop VATSPRCVN, phosphoribosylanthranilate isomerase, EC 5.3.1.24705140
Mut_L2_UreEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 2, sequence of loop GGTGPAAGTHATTCTPG, urease, EC 3.5.1.5705140
Mut_L4_ADAEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop GDELGFPGSLF, adenosine diaminase, EC 3.5.4.4705140
Mut_L4_alphaTSEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop DVPVQQS, tryptophan synthase, EC 4.2.1.20705140
Mut_L4_DHDPSEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop PYYNRPS, dihydrodipicolinate synthase, EC 4.2.1.52705140
Mut_L4_FBPAEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop DLSEES, fructose-bisphosphate aldolase, EC 4.1.2.13705140
Mut_L4_MREscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop EPTLEHD, mandelate racemase, EC 5.1.2.2705140
Mut_L4_PBGSEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop AAMDG, porphobilinogen synthase, EC 4.2.1.24705140
Mut_L4_PRAI_WTEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop GNEE, phosphoribosylanthranilate isomerase, EC 5.3.1.24705140
Mut_L4_TPSEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop LGQEDLH, thiamine-phosphate diphosphorylase, EC 2.5.1.3705140
Mut_L4_UreEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 4, sequence of loop EDWGAT, urease, EC 3.5.1.5705140
Mut_L6_alphaTSEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop SRAGVTGAENRAALP, tryptophan synthase, EC 4.2.1.20705140
Mut_L6_DHDPSEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop TGNL, dihydrodipicolinate synthase, EC 4.2.1.52705140
Mut_L6_PBGSEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop PAGAY, porphobilinogen synthase, EC 4.2.1.24705140
R139NStreptomyces coelicolorP16250mutant, used for crystallization, steady-state Michaelis-Menten enzyme kinetic is studied706633
R19AStreptomyces coelicolorP16250mutant, steady-state Michaelis-Menten enzyme kinetic is studied706633
S81TStreptomyces coelicolorP16250mutant, steady-state Michaelis-Menten enzyme kinetic is studied706633
C7AThermotoga maritimaQ56320catalytically inactive mutant648892
D126NThermotoga maritimaQ56320mutant with drastically reduced activity648892
additional informationArabidopsis thaliana-PAI deletion mutant trp6 shows abnormal growth and development, isolated from Wassilewskija ecotype, which contains 4 PAI isogenes, the only active isogene in trp6 is PAI2648888
Mut_L6_PRAI_WTEscherichia coli-loop exchange in the PRAI-LoxP scaffold, position beta/alpha loop 6, sequence of loop NGQGGSGQRFD, phosphoribosylanthranilate isomerase, EC 5.3.1.24705140
additional informationPhytophthora parasiticaP24920insertion mutagenesis of TRP1 gene648879
additional informationSaccharomyces cerevisiae-insertion of the cleavage sequence of human cytomegalovirus, HCMV, protease, which is an attractive target for antiviral drug development because of its essential function in viral replication, the enzyme serves as substrate for the protease in the screening assay for small molecule inhibitors of the protease, coexpression of HCMV protease with the engineered Trp1p substrate in yeast cells results in site-specific cleavage and functional inactivation of the Trp1p enzyme, thereby leading to an arrest of cell proliferation, this growth arrest can be suppressed by the addition of validated HCMV protease inhibitors, overview677592
D126N/C7AThermotoga maritima-catalytically inactive double mutant648886, 648892
additional informationThermotoga maritima-mutationally generated monomers of dimeric PRAI are as active as the dimer, but far more thermolabile, Pro-52/Phe-53 deletion mutant and mutants with multiple point mutations648886

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
biotechnologyEscherichia coli-the work provides a method of exchanging variably sized loops within the (beta/alpha)8 fold, affording a novel starting point for the screening of novel activities as well as modest diversions from an original activity705140

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
4593Hoch, S.O.Isolation and characterization of two tryptophan biosynthetic enzymes, indoleglycerol phosphate synthase and phosphoribosyl anthranilate isomerase, from Bacillus subtilisJ. Bacteriol.139362-3681979Bacillus subtilis, Bacillus subtilis T3 PubMed
4599Largen, M.; Belser, W.L.Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymesJ. Bacteriol.121239-2491975Aeromonas caviae, Citrobacter freundii, Citrobacter freundii NCTC 6021, Pectobacterium carotovorum, Pectobacterium carotovorum ICPB EC153, Proteus vulgaris, Serratia rubidaea PubMed
4601Potts, J.M.; Drapeau, G.R.Partial characterization of phosphoribosyl transferase, phosphoribosyl anthranilate isomerase, and indole glycerol phosphate synthase from Serratia marcescensJ. Bacteriol.111334-3391972Serratia marcescens, Serratia marcescens HY PubMed
4611Eberhard, M.; Tsai-Pflugfelder, M.; Bolewska, K.; Hommel, U.; Kirschner, K.Indoleglycerol phosphate synthase - phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domainsBiochemistry345419-54281995Escherichia coli, Saccharomyces cerevisiae, Saccharomyces cerevisiae xPRAI PubMed
638666Hommel, U.; Lustig, A.; Kirschner, K.Purification and characterization of yeast anthranilate phosphoribosyltransferaseEur. J. Biochem.18033-401989Escherichia coli, Saccharomyces cerevisiae PubMed
648868Creighton, T.E.; Yanofsky, C.Chorismate to tryptophan (Escherichia coli) - anthranilate synthethase, PR transferase; PRA isomerase, InGP synthetase, tryptophan synthetaseMethods Enzymol.17A365-3801970Escherichia coli-
648869Huetter, R.; Niederberger, P.; DeMoss, J.A.Tryptophan biosynthetic genes in eukaryotic microorganismsAnnu. Rev. Microbiol.4055-771986Coprinopsis lagopus, Coprinopsis radiata, Emericella nidulans, Escherichia coli, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe PubMed
648870Braus, G.H.; Luger, K.; Paravicini, G.; Schmidheini, T.; Kirschner, K.; Huetter, R.The role of the TRP1 gene in tryptophan biosynthesisJ. Biol. Chem.2637868-78751988Saccharomyces cerevisiae PubMed
648871Hankins, C.N.; Largen, M.T.; Mills, S.E.Some physical characteristics of the enzymes of L-tryptophan biosynthesis in higher plantsPlant Physiol.57101-1041976Pisum sativum, Zea mays PubMed
648872Kirschner, K.; Szadkowski, H.; Jardetzky, T.S.; Hager, V.Phosphoribosylanthranilate isomerase-indoleglycerol-phosphate synthase from Escherichia coliMethods Enzymol.142386-3971987Acinetobacter calcoaceticus, Bacillus subtilis, [Brevibacterium] flavum, Emericella nidulans, Escherichia coli, Escherichia coli W3110, Neurospora crassa, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens PubMed
648873Hommel, U.; Eberhard, M.; Kirschner, K.Phosphoribosyl anthranilate isomerase catalyzes a reversible amadori reactionBiochemistry345429-54391995Escherichia coli, Saccharomyces cerevisiae, Saccharomyces cerevisiae xPRAI PubMed
648874Arroyo-Begovich, A.; DeMoss, J.A.The isolation of the components of the anthranilate synthetase complex from Neurospora crassaJ. Biol. Chem.2481262-12671973Neurospora crassa PubMed
648875Bisswanger, H.; Kirschner, K.; Cohn, W.; Hager, V.; Hansson, E.N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 1. A Substrate analogue binds to two different binding sites on the bifunctional enzyme from Escherichia coliBiochemistry185946-59531979Escherichia coli, Escherichia coli W3110 PubMed
648876Priestle, J.P.; Gruetter, M.G.; White, J.L.; Vincent, M.G.; Kania, M; Wilson, E.; Jardetzky, T.S.; Kirschner, K.; Jansonius, J.N.Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coliProc. Natl. Acad. Sci. USA845690-56941987Escherichia coli PubMed
648877Walker, M.S.; DeMoss, J.A.Organisation of the functional domains of anthranilate synthase from Neurospora crassaJ. Biol. Chem.26116073-160771986Neurospora crassa PubMed
648879Karlovsky, P.; Prell, H.H.The TRP1 gene of Phytophora parasitica encoding indole-3-glycerolphosphate synthase-N-(5'-phossphoribosyl)anthranilate isomerase: structure and evolutionary distance from homologous fungal genesGene109161-1651991Phytophthora parasitica (P24920), Phytophthora parasitica PubMed
648880Lam, W.L.; Logan, S.M.; Doolittle, W.F.Genes for tryptophan biosynthesis in the halophilic archaebacterium Haloferax volcanii: the trpDFEG clusterJ. Bacteriol.1741694-16971992Haloferax volcanii PubMed
648883Bode, R.; Birnbaum, D.Die Enzyme der Biosynthese aromatischer Aminos„uren bei Hansenula henricii: Phosohoribosyl-Anthranilate-Isomerase und Indolglycerin-Phosphate-Synthase (E:C:4.1.1.48)Z. Allg. Mikrobiol.9629-6351978Hansenula henricii, Hansenula henricii CCY 38-10-2-
648885White, J.L.; Gruetter, M.G.; Wilson, E.; Thaller, C.; Ford, G.C.; Smit, J.D.G.; Jansonius, J.N.; Kirschner, K.Crystallization and preliminary X-ray crystallographic data of the bifunctional enzyme phosphoribosyl-anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coliFEBS Lett.14887-901982Escherichia coli-
648886Thoma, R.; Hennig, M.; Sterner, R.; Kirschner, K.Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritimaStructure8265-2762000Thermotoga maritima PubMed
648887Sterner, R.; Kleemann, G.R.; Szadkowski, H.; Lustig, A.; Hennig, M.; Kirschner, K.Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimerProtein Sci.52000-20081996Thermotoga maritima PubMed
648888He, Y.; Li, J.Differential expression of triplicate phosphoribosylanthranilate isomerase isogenes in the tryptophan biosynthetic pathway of Arabidopsis thaliana (L.) Heynh.Planta212641-6472001Arabidopsis thaliana PubMed
648889Hennig, M.; Sterner, R.; Kirschner, K.; Jansonius, J.N.Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stabilityBiochemistry366009-60161997Thermotoga maritima (Q56320), Thermotoga maritima PubMed
648890Sterner, R.; Merz, A.; Thoma, R.; Kirschner, K.Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritimaMethods Enzymol.331270-2802001Thermotoga maritima PubMed
648892Henn-Sax, M.; Thoma, R.; Schmidt, S.; Hennig, M.; Kirschner, K.; Sterner, R.Two (betaalpha)8-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substratesBiochemistry4112032-120422002Thermotoga maritima, Thermotoga maritima (Q56320) PubMed
660613Wright, H.; Barona-Gomez, F.; Hodgson, D.A.; Fueloep, V.Expression, purification and preliminary crystallographic analysis of phosphoribosyl isomerase (PriA) from Streptomyces coelicolorActa Crystallogr. Sect. DD60534-5362004Streptomyces coelicolor PubMed
661544Staats, C.C.; Silva, M.S.N.; Pinto, P.M.; Vainstein, M.H.; Schrank, A.The Metarhizium anisopliae trp1 gene: Cloning and regulatory analysisCurr. Microbiol.4966-702004Metarhizium anisopliae, Metarhizium anisopliae (Q873X5) PubMed
662064Taka, J.; Ogasahara, K.; Jeyakanthan, J.; Kunishima, N.; Kuroishi, C.; Sugahara, M.; Yokoyama, S.; Yutani, K.Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experimentsJ. Biochem.137569-5782005Thermus thermophilus HB8 (P83825), Thermus thermophilus HB8 PubMed
662618Leopoldseder, S.; Claren, J.; Jurgens, C.; Sterner, R.Interconverting the catalytic activities of (betaalpha)(8)-barrel enzymes from different metabolic pathways: sequence requirements and molecular analysisJ. Mol. Biol.337871-8792004Thermotoga maritima PubMed
677592Cottier, V.; Barberis, A.; Luethi, U.Novel yeast cell-based assay to screen for inhibitors of human cytomegalovirus protease in a high-throughput formatAntimicrob. Agents Chemother.50565-5712006Saccharomyces cerevisiae PubMed
693634Patrick, W.M.; Matsumura, I.A study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomeraseJ. Mol. Biol.377323-3362008Escherichia coli PubMed
693660Akanuma, S.; Yamagishi, A.Experimental evidence for the existence of a stable half-barrel subdomain in the (beta/alpha)8-barrel foldJ. Mol. Biol.382458-4662008Escherichia coli, Escherichia coli (P00909) PubMed
705140Ochoa-Leyva, A.; Soberon, X.; Sanchez, F.; Argueello, M.; Montero-Moran, G.; Saab-Rincon, G.Protein design through systematic catalytic loop exchange in the (beta/alpha)8 foldJ. Mol. Biol.387949-9642009Escherichia coli (P00909) PubMed
706633Noda-Garcia, L.; Camacho-Zarco, A.R.; Verdel-Aranda, K.; Wright, H.; Soberon, X.; Fueloep, V.; Barona-Gomez, F.Identification and analysis of residues contained on beta --> alpha loops of the dual-substrate (beta alpha)8 phosphoribosyl isomerase A specific for its phosphoribosyl anthranilate isomerase activityProtein Sci.19535-5432010Streptomyces coelicolor (P16250), Streptomyces coelicolor PubMed
715931Setiyaputra, S.; Mackay, J.P.; Patrick, W.M.The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the (betaalpha)8 barrel foldJ. Mol. Biol.408291-3032011Escherichia coli (P00909) PubMed
716884Akanuma, S.; Yamagishi, A.Roles for the two N-terminal (beta/alpha) modules in the folding of a (beta/alpha)8-barrel protein as studied by fragmentation analysisProteins79221-2312011Escherichia coli PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 5.3.1.24)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)