Information on EC 2.7.7.75 - molybdopterin adenylyltransferase:

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota


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EC NUMBERCOMMENTARY
2.7.7.75-

RECOMMENDED NAMEGeneOntology No.
molybdopterin adenylyltransferaseGO:0061598

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
show the reaction diagram
----
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
show the reaction diagram
comparative analyses reveal a possible role for the N- and C-terminal residues of MoaB and MogA proteins, respectively, in stabilizing the substrate and/or product molecule in the active siteAquifex aeolicusQ5SLF2723849

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
nucleotidyl group transferEscherichia coliP0AF03-708986
nucleotidyl group transferArabidopsis thalianaQ39054-708983, 710443

PATHWAYKEGG LinkMetaCyc Link
molybdenum cofactor biosynthesis-PWY-6823

SYSTEMATIC NAMEIUBMB Comments
ATP:molybdopterin adenylyltransferaseCatalyses the activation of molybdopterin for molybdenum insertion. In eukaryotes, this reaction is catalysed by the C-terminal domain of a fusion protein that also includes molybdopterin molybdotransferase (EC 2.10.1.1). The reaction requires a divalent cation such as Mg2+ or Mn2+.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
AaMogAAquifex aeolicusQ5SLF2-723849
Cnx1Arabidopsis thalianaQ39054C-terminal G-domain, gene name708983, 710443
MogAEscherichia coliP0AF03gene name708986

CAS REGISTRY NUMBERCOMMENTARY
No entries in this field

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Aquifex aeolicus-723849Q5SLF2UniProtManually annotated by BRENDA team
Arabidopsis thalianadomain G; commentary708983, 710443Q39054SwissProtManually annotated by BRENDA team
Escherichia coliK-12708986P0AF03SwissProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismEscherichia coliP0AF03molybdenum cofactor biosynthesis708986
metabolismArabidopsis thalianaQ39054molybdenum cofactor biosynthesis708983, 710443

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + molybdopterindiphosphate + adenylyl-molybdopterin
show the reaction diagram
Arabidopsis thalianaQ39054-708983--?
ATP + molybdopterindiphosphate + adenylyl-molybdopterin
show the reaction diagram
Arabidopsis thaliana--710443--?
ATP + molybdopterindiphosphate + adenylyl-molybdopterin
show the reaction diagram
Escherichia coliP0AF03-708986--?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + molybdopterindiphosphate + adenylyl-molybdopterin
show the reaction diagram
Arabidopsis thalianaQ39054-708983--?
ATP + molybdopterindiphosphate + adenylyl-molybdopterin
show the reaction diagram
Arabidopsis thaliana--710443--?
ATP + molybdopterindiphosphate + adenylyl-molybdopterin
show the reaction diagram
Escherichia coliP0AF03-708986--?

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Mg2+Arabidopsis thaliana-required708983
Mg2+Escherichia coliP0AF03required708986
Mn2+Arabidopsis thaliana-required708983

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
diphosphateArabidopsis thaliana-efficient inhibition at 1-10 mM diphosphate708983 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
diphosphateArabidopsis thaliana-activating by 5 units in the standard reaction set-up708983 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.062-ATPArabidopsis thaliana-10 mM MgCl2, pH 7.2, temperature not specified in the publication708983 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0012-ATPArabidopsis thaliana-10 mM MgCl2, pH 7.2, temperature not specified in the publication708983 2D-image

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
1di6, downloadSCOP (1di6)CATH (1di6)Escherichia coli (strain K12)
1di7, downloadSCOP (1di7)CATH (1di7)Escherichia coli (strain K12)
4lhb, downloadSCOP (4lhb)CATH (4lhb)Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
oligomerAquifex aeolicusQ5SLF2-723849

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

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
crystal structure of AaMogA is determined at 1.7 A resolution (space group P2 resolution), or 1.9 A resolution (space group P1)Aquifex aeolicusQ5SLF2723849

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
using Ni-NTA chromatographyAquifex aeolicusQ5SLF2723849
Ni-nitrilotriacetic acid matrixArabidopsis thalianaQ39054708983, 710443

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expressed in Escherichia coli as a His-tagged fusion proteinAquifex aeolicusQ5SLF2723849
Cnx1 G-domain in pQE60Arabidopsis thalianaQ39054708983, 710443

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

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D486AArabidopsis thaliana-inactive708983
D515HArabidopsis thaliana-inactive708983
D515HArabidopsis thaliana-in Cnx1 G-domain, accumulation of molybdopterin710443
D515NArabidopsis thaliana-in Cnx1 G-domain, accumulation of molybdopterin710443
N597LArabidopsis thaliana-in Cnx1 G-domain, strong decrease in molybdopterin binding710443
R547EArabidopsis thaliana-decreased activity708983
S476AArabidopsis thaliana-inactive708983
S573AArabidopsis thaliana-inactive in absence of pyrophosphatase, decreased actitivity in presence of pyrophosphatase708983
S583AArabidopsis thaliana-increased activity708983
T542AArabidopsis thaliana-decreased activity708983
T542DArabidopsis thaliana-inactive708983
T542SArabidopsis thaliana-decreased activity708983
V557GArabidopsis thaliana-in Cnx1 G-domain, strong decrease in molybdopterin binding710443

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 ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
708983Llamas, A.; Mendel, R.R.; Schwarz, G.Synthesis of adenylated molybdopterin: an essential step for molybdenum insertionJ. Biol. Chem.27955241-552462004Arabidopsis thaliana, Arabidopsis thaliana (Q39054) PubMed
708986Nichols, J.D.; Rajagopalan, K.V.In vitro molybdenum ligation to molybdopterin using purified componentsJ. Biol. Chem.2807817-78222005Escherichia coli (P0AF03), Escherichia coli (P12281) PubMed
710443Kuper, J.; Palmer, T.; Mendel, R.R.; Schwarz, G.Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin binding, molybdenum insertion, and molybdenum cofactor stabilizationProc. Natl. Acad. Sci. USA976475-64802000Arabidopsis thaliana, Arabidopsis thaliana (Q39054) PubMed
723849Kanaujia, S.P.; Jeyakanthan, J.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Sekar, K.Crystal structures, dynamics and functional implications of molybdenum-cofactor biosynthesis protein MogA from two thermophilic organismsActa Crystallogr. Sect. F672-162011Aquifex aeolicus, Aquifex aeolicus (Q5SLF2) PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.7.7.75)
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)