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Information on EC 6.3.2.6 - phosphoribosylaminoimidazolesuccinocarboxamide synthase and Organism(s) Pyrococcus horikoshii and UniProt Accession O57978

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IUBMB Comments
Forms part of the purine biosynthesis pathway.
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This record set is specific for:
Pyrococcus horikoshii
UNIPROT: O57978
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
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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PH0239
locus name
phosphoribosylaminoimidazole-succinocarboxamide synthetase
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Phosphoribosylaminoimidazolesuccinocarboxamide synthetase
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SAICAR synthetase
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the de novo purine biosynthesis pathway
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-crystallization of SAICAR synthetase from Pyrococcus horikoshii with substrates and other nucleotides produces eight ligand bound structures, five in C2221 and three in H3 space groups. These ligand bound complexes have minor structural deviations compared to their corresponding apo structures. In most of the structures the hydrolyzed product of the nucleotide triphosphates are bound to the enzyme
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Manjunath, K.; Kanaujia, S.P.; Kanagaraj, S.; Jeyakanthan, J.; Sekar, K.
Structure of SAICAR synthetase from Pyrococcus horikoshii OT3: insights into thermal stability
Int. J. Biol. Macromol.
53
7-19
2013
Pyrococcus horikoshii (O57978), Pyrococcus horikoshii OT-3 (O57978)
Manually annotated by BRENDA team
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
Manjunath, K.; Jeyakanthan, J.; Sekar, K.
Catalytic pathway, substrate binding and stability in SAICAR synthetase: A structure and molecular dynamics study
J. Struct. Biol.
191
22-31
2015
Pyrococcus horikoshii (O57978), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O57978)
Manually annotated by BRENDA team