Information on EC 5.3.3.17 - trans-2,3-dihydro-3-hydroxyanthranilate isomerase:
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EC NUMBERCOMMENTARY
5.3.3.17-

RECOMMENDED NAMEGeneOntology No.
trans-2,3-dihydro-3-hydroxyanthranilate isomerase-

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate = (1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram		----
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate = (1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram		-Pseudomonas fluorescens-702206

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

PATHWAYKEGG LinkMetaCyc Link
phenazine-1-carboxylate biosynthesis-PWY-5770

SYSTEMATIC NAMEIUBMB Comments
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate isomeraseThe enzyme is involved in phenazine biosynthesis.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
phzFPseudomonas fluorescens-gene name701459, 702206, 706479

CAS REGISTRY NUMBERCOMMENTARY
No entries in this field

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Pseudomonas fluorescens-706479Q51792SwissProtManually annotated by BRENDA team
Pseudomonas fluorescensstrain 2-79701459, 702206Q51792SwissProtManually annotated by BRENDA team
Pseudomonas fluorescens Feb 79strain 2-79701459Q51792SwissProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram		Pseudomonas fluorescens-i.e. trans-2,3-dihydro-3-hydroxyanthranilic acid702206i.e. 2,3-dihydro-3-hydroxy-anthranilate-?
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram		Pseudomonas fluorescensQ51792i.e. trans-2,3-dihydro-3-hydroxyanthranilic acid. The enzyme is involved in phenazine synthesis706479i.e. 2,3-dihydro-3-hydroxy-anthranilate-?
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram		Pseudomonas fluorescensQ51792charactierzation of the product by NMR spectrometry. The structure of PhzF in complex with its substrate, trans-2,3-dihydro-3-hydroxyanthranilic acid, suggests that it is an isomerase using the conserved glutamate45 to abstract a proton from C3 of the substrate. The proposed mechanism involves proton abstraction from C3 of trans-2,3-dihydro-3-hydroxyanthranilate by Glu45, followed by rearrangement of the double bonds and reprotonation at C1. The function of E45 as a proton shuttle is supported by results from NMR spectroscopy706479--?
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram		Pseudomonas fluorescens-PhzF is capable of producing phenazine-1-carboxylic acid, albeit slowly, from trans-2,3-dihydro-3-hydroxyanthranilic acid (i.e. (5S,6R)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxylic acid). These observations suggest that PhzF catalyzes the initial step in the conversion of trans-2,3-dihydro-3-hydroxyanthranilic acid to phenazine-1-carboxylic acid, probably via a rearrangement reaction yielding the more reactive 3-oxo analogue of trans-2,3-dihydro-3-hydroxyanthranilic acid, and that subsequent steps can occur spontaneously. A hypothetical model for how trans-2,3-dihydro-3-hydroxyanthranilic acid binds to the PhzF active site suggests that Glu45 and Asp208 could act as general acid-base catalysts in a rearrangement reaction702206i.e. 2,3-dihydro-3-hydroxy-anthranilate-?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram		Pseudomonas fluorescens-i.e. trans-2,3-dihydro-3-hydroxyanthranilic acid702206i.e. 2,3-dihydro-3-hydroxy-anthranilate-
(5S,6S)-6-amino-5-hydroxycyclohexane-1,3-diene-1-carboxyate(1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate
show the reaction diagram		Pseudomonas fluorescensQ51792i.e. trans-2,3-dihydro-3-hydroxyanthranilic acid. The enzyme is involved in phenazine synthesis706479i.e. 2,3-dihydro-3-hydroxy-anthranilate-

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
No entries in this field

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
No entries in this field

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

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
No entries in this field

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
No entries in this field

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

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

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

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
No entries in this field

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

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
32000-Pseudomonas fluorescens-two protein species with MW 32048 Da and 32224 Da, MALDI-TOF mass-spectrometry701459
42000-Pseudomonas fluorescensQ51792gel filtration706479
66070-Pseudomonas fluorescens-laser light scattering in solution702206

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerPseudomonas fluorescens-2 * 32218, histidine-tagged enzyme702206
dimerPseudomonas fluorescensQ51792deduced from crystal structure. The crystal structure clarifies that the enzyme is a dimer in an up/up configuration with the two active sites facing each other. The dimer in the open form, generates by crystal symmetry (sulfate complex), interacts mainly through the alpha1-helices and the beta16-strands in the N-terminal domains. The C-terminal domains are not in direct contact but are relatively close706479

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

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
1.8 A crystal structure of PhzF, hanging drop vapor diffusion methodPseudomonas fluorescens-702206
hanging-drop vapor-diffusion method. Crystals of unliganded PhzF belong to space group P3(2)21 with a a = b = 56 A, and c = 156 A and hold one monomer per asymmetric unit. Complexes of PhzF (with 3-hydroxyanthranilic acid and trans-2,3-dihydro-3-hydroxyanthranilic acid) crystallize in space group P2(1)2(1)2 with cell parameters of a = 93 A, b = 100 A, and c = 57 A and contain one dimer in the asymmetric unitPseudomonas fluorescensQ51792706479
hanging-drop vapour-diffusion method. Crystallized from PEG 4000/ammonium sulfate/sodium citrate pH 5.6. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 56.3, c = 156.4 A. They contain one monomer in the asymmetric unit and diffract to better than 1.7 A on synchrotron beamlines. Crystals of seleno-L-methionine-labelled PhzF have been obtainedPseudomonas fluorescens-701459

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

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

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Pseudomonas fluorescens-701459, 702206, 706479

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coliPseudomonas fluorescens-702206, 706479
large-scale expression in Escherichia coliPseudomonas fluorescens-701459

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

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

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

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
701459Mavrodi, D.V.; Bleimling, N.; Thomashow, L.S.; Blankenfeldt, W.The purification, crystallization and preliminary structural characterization of PhzF, a key enzyme in the phenazine-biosynthesis pathway from Pseudomonas fluorescens 2-79Acta Crystallogr. Sect. D60184-1862004Pseudomonas fluorescens PubMed
702206Parsons, J.F.; Song, F.; Parsons, L.; Calabrese, K.; Eisenstein, E.; Ladner, J.E.Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79Biochemistry4312427-124352004Pseudomonas fluorescens PubMed
706479Blankenfeldt, W.; Kuzin, A.P.; Skarina, T.; Korniyenko, Y.; Tong, L.; Bayer, P.; Janning, P.; Thomashow, L.S.; Mavrodi, D.V.Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescensProc. Natl. Acad. Sci. USA10116431-164362004Pseudomonas fluorescens PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 5.3.3.17)
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)