EzCatDB: D00298
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DB codeD00298
CATH domainDomain 13.30.200.20 : Phosphorylase Kinase; domain 1
Domain 23.30.470.20 : D-amino Acid Aminotransferase; Chain A, domain 1
E.C.6.3.2.6

CATH domainRelated DB codes (homologues)
3.30.200.20 : Phosphorylase Kinase; domain 1M00125,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 1T00082,M00035,M00037,M00051,T00107,T00108

Enzyme Name
UniProtKBKEGG

P27616
Protein namePhosphoribosylaminoimidazole-succinocarboxamide synthasephosphoribosylaminoimidazolesuccinocarboxamide 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
SynonymsEC 6.3.2.6
SAICAR synthetase
RefSeqNP_009409.1 (Protein)
NM_001178216.1 (DNA/RNA sequence)
PfamPF01259 (SAICAR_synt)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00230Purine metabolism

UniProtKB:Accession NumberP27616
Entry namePUR7_YEAST
ActivityATP + 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.
SubunitMonomer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00002C04751C00049C00008C00009C04823
CompoundMagnesiumATP1-(5'-Phosphoribosyl)-5-amino-4-carboxyimidazoleL-AspartateADPOrthophosphate1-(5'-Phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotideamine group,carboxyl group,nucleotideamino acids,carboxyl groupamine group,nucleotidephosphate group/phosphate ionamino acids,amide group,amine group,carbohydrate,nucleotide
ChEBI18420
15422
28413
17053
16761
26078
18319
PubChem888
5957
165388
5960
44367445
6022
22486802
1004
160666
               
1a48A01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1a48A02UnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P27616
pdb
        
1a48A01
1a48A02


references
[1]
PubMed ID1534690
JournalBiochemistry
Year1992
Volume31
Pages5022-32
AuthorsMeyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM
TitlePurification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway.
[2]
PubMed ID1447788
JournalJ Mol Biol
Year1992
Volume228
Pages298-9
AuthorsGrebenko AI, Levdikov VM, Barynin VV, Melik-Adamyan WR, Myasnikov AN
TitleCrystallization and preliminary X-ray investigation of phosphoribosylaminoimidazolesuccinocarboxamide synthase from the yeast Saccharomyces cerevisiae.
[3]
PubMed ID7918411
JournalBiochemistry
Year1994
Volume33
Pages11927-34
AuthorsFirestine SM, Poon SW, Mueller EJ, Stubbe J, Davisson VJ
TitleReactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID98212921
PubMed ID9551557
JournalStructure
Year1998
Volume6
Pages363-76
AuthorsLevdikov VM, Barynin VV, Grebenko AI, Melik-Adamyan WR, Lamzin VS, Wilson KS
TitleThe structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis.
Related PDB1a48
Related UniProtKBP27616


createdupdated
2004-03-252009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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