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InterPro: IPR001636 SAICAR synthetase

Protein matchesHelp
UniProtKB
Matches:
1901 proteins
AccessionHelp IPR001636 SAICAR_synt
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR014106 Phosphoribosylaminoimidazole-succinocarboxamide synthase
Contains IPR013816 ATP-grasp fold, subdomain 2
IPR018236 SAICAR synthetase, conserved site
GO Term annotationHelp
Process GO:0006164 purine nucleotide biosynthetic process
Function GO:0004639 phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC:6.3.2.6) (SAICAR synthetase) catalyzes the seventh step in the de novo purine biosynthetic pathway; the ATP-dependent conversion of 5'-phosphoribosyl-5-aminoimidazole-4-carboxylic acid and aspartic acid to SAICAR [1].

In bacteria (purC), fungi (ADE1) and plants (Pur7), SAICAR synthetase is a monofunctional protein; in animals it is the N-terminal domain of a bifunctional enzyme that also catalyse phosphoribosylaminoimidazole carboxylase (AIRC) activity (see IPR000031).

Structural linksHelp
SCOP: d.143.1.1
Database linksHelp
PDBe-motif: PS01057 , PS01058
Enzyme: EC:6.3.2.6
PROSITE doc: PDOC00810
PANDIT: PF01259
Blocks: IPB001636

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001636 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P22234 Multifunctional protein ADE2

P27616 Phosphoribosylaminoimidazole-succinocarboxamide synthase

Q10457 Probable multifunctional protein ADE2

Q9DCL9 Multifunctional protein ADE2

Q9I7S8 Multifunctional protein ADE2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000031 1-(5-Phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR) carboxylase
IPR018236 SAICAR synthetase, conserved site
IPR013816 ATP-grasp fold, subdomain 2
IPR001636 SAICAR synthetase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Zalkin H, Dixon JE.
De novo purine nucleotide biosynthesis.
Prog. Nucleic Acid Res. Mol. Biol. 42 259-87 1992 [PubMed: 1574589]

Additional ReadingHelp
Zhang R, Skarina T, Evdokimova E, Edwards A, Savchenko A, Laskowski R, Cuff ME, Joachimiak A.
Structure of SAICAR synthase from Thermotoga maritima at 2.2 angstroms reveals an unusual covalent dimer.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 2006 335-9 [PubMed: 16582479]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=16582479
Levdikov VM, Barynin VV, Grebenko AI, Melik-Adamyan WR, Lamzin VS, Wilson KS.
The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis.
Structure 6 1998 363-76 [PubMed: 9551557]
http://dx.doi.org/10.1016/S0969-2126(98)00038-0
Ginder ND, Binkowski DJ, Fromm HJ, Honzatko RB.
Nucleotide complexes of Escherichia coli phosphoribosylaminoimidazole succinocarboxamide synthetase.
J. Biol. Chem. 281 2006 20680-8 [PubMed: 16687397]
http://dx.doi.org/10.1074/jbc.M602109200
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InterPro 23.1