DB code: D00298

CATH domain 3.30.200.20 : Phosphorylase Kinase; domain 1
3.30.470.20 : D-amino Acid Aminotransferase; Chain A, domain 1
E.C. 6.3.2.6
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.30.200.20 : Phosphorylase Kinase; domain 1 M00125 M00124 M00131 T00224 M00127 M00129 M00130 M00132 M00136 M00196 M00197 M00198 M00304 M00323 M00325 M00326 M00327 M00328 M00329 M00330 M00331 M00332 M00333 M00335 M00339 M00344
3.30.470.20 : D-amino Acid Aminotransferase; Chain A, domain 1 T00082 M00035 M00037 M00051 T00107 T00108

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P27616 Phosphoribosylaminoimidazole-succinocarboxamide synthase
EC 6.3.2.6
SAICAR synthetase
NP_009409.1 (Protein)
NM_001178216.1 (DNA/RNA sequence)
PF01259 (SAICAR_synt)
[Graphical View]

KEGG enzyme name
phosphoribosylaminoimidazolesuccinocarboxamide synthase
phosphoribosylaminoimidazole-succinocarboxamide synthetase
PurC
SAICAR synthetase
4-(N-succinocarboxamide)-5-aminoimidazole synthetase
4-[(N-succinylamino)carbonyl]-5-aminoimidazole ribonucleotidesynthetase
SAICARs
phosphoribosylaminoimidazolesuccinocarboxamide synthetase
5-aminoimidazole-4-N-succinocarboxamide ribonucleotide synthetase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P27616 PUR7_YEAST 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. Monomer.

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C04751 C00049 C00008 C00009 C04823
E.C.
Compound Magnesium ATP 1-(5'-Phosphoribosyl)-5-amino-4-carboxyimidazole L-Aspartate ADP Orthophosphate 1-(5'-Phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide amine group,carboxyl group,nucleotide amino acids,carboxyl group amine group,nucleotide phosphate group/phosphate ion amino acids,amide group,amine group,carbohydrate,nucleotide
ChEBI 18420
18420
15422
15422
28413
28413
17053
17053
16761
16761
26078
26078
18319
18319
PubChem 888
888
5957
5957
165388
165388
44367445
5960
44367445
5960
6022
6022
1004
22486802
1004
22486802
160666
160666
1a48A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1a48A02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P27616

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1a48A01
1a48A02

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 1534690
Journal Biochemistry
Year 1992
Volume 31
Pages 5022-32
Authors Meyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM
Title Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1447788
Journal J Mol Biol
Year 1992
Volume 228
Pages 298-9
Authors Grebenko AI, Levdikov VM, Barynin VV, Melik-Adamyan WR, Myasnikov AN
Title Crystallization and preliminary X-ray investigation of phosphoribosylaminoimidazolesuccinocarboxamide synthase from the yeast Saccharomyces cerevisiae.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7918411
Journal Biochemistry
Year 1994
Volume 33
Pages 11927-34
Authors Firestine SM, Poon SW, Mueller EJ, Stubbe J, Davisson VJ
Title Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID 98212921
PubMed ID 9551557
Journal Structure
Year 1998
Volume 6
Pages 363-76
Authors Levdikov VM, Barynin VV, Grebenko AI, Melik-Adamyan WR, Lamzin VS, Wilson KS
Title The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis.
Related PDB 1a48
Related UniProtKB P27616

Comments

Created Updated
2004-03-25 2009-02-26