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Information on EC 2.7.7.80 - molybdopterin-synthase adenylyltransferase and Organism(s) Homo sapiens and UniProt Accession O95396

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IUBMB Comments
Adenylates the C-terminus of the small subunit of the molybdopterin synthase. This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit. The reaction occurs in prokaryotes and eukaryotes. In the human, the reaction is catalysed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.
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Homo sapiens
UNIPROT: O95396
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
mocs3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molybdenum cofactor synthesis protein 3
UniProt
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:molybdopterin-synthase adenylyltransferase
Adenylates the C-terminus of the small subunit of the molybdopterin synthase. This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit. The reaction occurs in prokaryotes and eukaryotes. In the human, the reaction is catalysed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly
diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly
diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
in homozygous MOCS3-knockout HEK293T cells, sulfite oxidase activity is almost completely abolished, on the basis of the absence of Moco in these cells. In addition, mcm5s2U thio-modified tRNAs are not detectable. Impact of a MOCS3 knockout on the cellular localization of NFS1, MOCS3-independent localization of NFS1 (a L-cysteine desulfurase NFS1 acting as a sulfur donor for MOCS3 in the cytosol) at the tips of the centrosome
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOCS3_HUMAN
460
0
49669
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C239A
the MOCS3 N-terminal domain mutant shows 81% reduced MoeB-like activity compared to wild-type MOCS3, the cysteine 293 residue in the MOCS3-MoeB domain is involved in the sulfur transfer reaction of MOCS3, EC 2.8.1.11
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the MOCS3 MoeB-like domain MOCS3-MoeBD in a Esccherichia coli MoeB-deficient strain moeB- (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matthies, A.; Nimtz, M.; Leimkhler, S.
Molybdenum cofactor biosynthesis in humans: Identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry
Biochemistry
44
7912-7920
2005
Homo sapiens (O95396), Homo sapiens
Manually annotated by BRENDA team
Matthies, A.; Rajagopalan, K.; Mendel, R.; Leimkhler, S.
Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans
Proc. Natl. Acad. Sci. USA
101
5946-5951
2004
Homo sapiens (O95396), Homo sapiens
Manually annotated by BRENDA team
Neukranz, Y.; Kotter, A.; Beilschmidt, L.; Marelja, Z.; Helm, M.; Graef, R.; Leimkuehler, S.
Analysis of the cellular roles of MOCS3 identifies a MOCS3-independent localization of NFS1 at the tips of the centrosome
Biochemistry
58
1786-1798
2019
Homo sapiens (O95396), Homo sapiens
Manually annotated by BRENDA team