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Information on EC 6.3.2.6 - phosphoribosylaminoimidazolesuccinocarboxamide synthase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58987

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IUBMB Comments
Forms part of the purine biosynthesis pathway.
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This record set is specific for:
Methanocaldococcus jannaschii
UNIPROT: Q58987
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Synonyms
saicar synthetase, saicar synthase, phosphoribosylaminoimidazole succinocarboxamide synthetase, airc-saicars, phosphoribosylaminoimidazole-succinocarboxamide synthase, phosphoribosylaminoimidazolesuccinocarboxamide synthetase, phosphoribosylaminoimidazole-succinocarboxamide synthetase, sppurc, bapurc, phosphoribosylaminoimidazolesuccinocarboxamide synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-Aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase
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N-(5-Amino-1-ribosyl-4-imidazolylcarbonyl)-L-aspartic acid 5´-phosphate synthetase
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Phosphoribosylaminoimidazolesuccinocarboxamide synthetase
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SAICAR synthetase
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Succino-AICAR synthetase
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Synthetase, phosphoribosylaminoimidazolesuccinocarboxamide
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VEG286A
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Vegetative protein 286A
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide formation
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carboxamide formation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate:L-aspartate ligase (ADP-forming)
Forms part of the purine biosynthesis pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-67-0
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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-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
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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 + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
delineation of the mesophilic (Escherichia coli, Ehrlichia chaffeensis), thermophilic (Geobacillus kaustophilus), and hyperthermophilic (Methanocaldococcus jannaschii, Pyrococcus horikoshii) proteins on the basis of their thermal stability by studying their dynamic aspects at 27°C and 60°C using molecular dynamics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Manjunath, K.; Sekar, K.
Molecular dynamics perspective on the protein thermal stability: a case study using SAICAR synthetase
J. Chem. Inf. Model.
53
2448-2461
2013
Escherichia coli, Ehrlichia chaffeensis, Geobacillus kaustophilus, Pyrococcus horikoshii (O57978), Methanocaldococcus jannaschii (Q58987), Pyrococcus horikoshii DSM 12428 (O57978), Methanocaldococcus jannaschii DSM 2661 (Q58987)
Manually annotated by BRENDA team