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Information on EC 6.3.5.3 - phosphoribosylformylglycinamidine synthase and Organism(s) Homo sapiens and UniProt Accession O15067

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Homo sapiens
UNIPROT: O15067 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
fgam synthetase, fgams, fgar-at, fgarat, orf75c, formylglycinamide ribonucleotide amidotransferase, phosphoribosylformylglycinamidine synthase, fgar amidotransferase, smpurl, tmpurl, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-Formamido-N-ribosylacetamide 5'-phosphate:L-glutamine amido-ligase (adenosine diphosphate)
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FGAM synthase
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FGAM synthetase
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FGAMS
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FGAR amidotransferase
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FGARAT
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Formylglycinamide ribonucloetide amidotransferase
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Formylglycinamide ribotide amidotransferase
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Formylglycinamide ribotide synthetase
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Phosphoribosylformylglycinamidine synthetase
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Phosphoribosylformylglycineamidine synthetase
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Synthetase, phosphoribosylformylglycinamide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
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amide group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide:L-glutamine amido-ligase (ADP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9032-84-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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increased activity in replicating cells and in tumors
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in fibroblasts infected with the human pathogen herpes simplex virus 1, FGAMS immunolabeling shifts from a diffuse cytoplasmic location to a mainly perinuclear localization by 12 hours post infection. In infected rat neurons, FGAMS localization shows no discernable changes. There are no changes in total FGAMS protein levels in either cell type
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PUR4_HUMAN
1338
0
144734
Swiss-Prot
other Location (Reliability: 5)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
in fibroblasts infected with the human pathogen herpes simplex virus 1, FGAMS immunolabeling shifts from a diffuse cytoplasmic location to a mainly perinuclear localization by 12 hours post infection. In infected rat neurons, FGAMS localization shows no discernable changes. There are no changes in total FGAMS protein levels in either cell type
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Elliott, W.L.; Weber, G.
Proliferation-linked increase in phosphoribosylformylglycinamidine synthetase activity
Cancer Res.
44
2430-2434
1984
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Mangold, C.A.; Yao, P.J.; Du, M.; Freeman, W.M.; Benkovic, S.J.; Szpara, M.L.
Expression of the purine biosynthetic enzyme phosphoribosyl formylglycinamidine synthase (FGAMS) in neurons
J. Neurochem.
144
723-735
2018
Rattus norvegicus, Homo sapiens (O15067), Homo sapiens
Manually annotated by BRENDA team