PUR7_PYRCJ
ID PUR7_PYRCJ Reviewed; 240 AA.
AC A3MXE4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000255|HAMAP-Rule:MF_00137};
DE EC=6.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00137};
DE AltName: Full=SAICAR synthetase {ECO:0000255|HAMAP-Rule:MF_00137};
GN Name=purC {ECO:0000255|HAMAP-Rule:MF_00137}; OrderedLocusNames=Pcal_1895;
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00137};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_00137}.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00137}.
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DR EMBL; CP000561; ABO09311.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MXE4; -.
DR SMR; A3MXE4; -.
DR STRING; 410359.Pcal_1895; -.
DR EnsemblBacteria; ABO09311; ABO09311; Pcal_1895.
DR KEGG; pcl:Pcal_1895; -.
DR eggNOG; arCOG04421; Archaea.
DR HOGENOM; CLU_061495_0_0_2; -.
DR OMA; EFCYKND; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR CDD; cd01415; SAICAR_synt_PurC; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR033934; SAICAR_synt_PurC.
DR Pfam; PF01259; SAICAR_synt; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..240
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000018764"
SQ SEQUENCE 240 AA; 26555 MW; D5A2FE6E70C9F5A5 CRC64;
MGFMELVYEG KAKAVYKTRE GLLMVFKDEV TAGDGARRDK APGKGALAAE TSTLLFQYLQ
GRGVTTHYLM FVPPNAILVK PAQVPPLEVI VRFKAYGSYL KRMPKAKPLT PFAKPIVEFH
YKDDSLHDPL ILEDDVVEAG LLTAGELAAV KDMALRAASA LRELYASVDC DFVDVKFEFG
RVGGELVLVD EVSGDTFRLL CGGEHFDKEY YRKTGDAVGL VERYAKLLEL TKLALSRQKV