ID   PUR7_SHEPW              Reviewed;         367 AA.
AC   B8CR57;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, 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=swp_3011;
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877;
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ29729.1; -; Genomic_DNA.
DR   RefSeq; WP_020913083.1; NC_011566.1.
DR   AlphaFoldDB; B8CR57; -.
DR   SMR; B8CR57; -.
DR   STRING; 225849.swp_3011; -.
DR   EnsemblBacteria; ACJ29729; ACJ29729; swp_3011.
DR   KEGG; swp:swp_3011; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_064197_0_0_6; -.
DR   OMA; QKARPVM; -.
DR   OrthoDB; 1345271at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000000753; 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   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR014106; SAICAR_synthase_Vibrio-typ.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   TIGRFAMs; TIGR02735; purC_vibrio; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..367
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_1000117852"
SQ   SEQUENCE   367 AA;  41309 MW;  EE053A051C4647E4 CRC64;
     MNLADKVLVV NDNLPIRTDK PVHSGKVRSV YWLTPEDSAR LIKDKGYDVP ADAPLAIMVI
     SDRISAFDCV WQGENGLNGV PGKGTALNAI SNHWFKLFKE KGLADSHILD IPHPLVWIVQ
     KARPVMIEAI ARQYITGSMW RSYTKGEREF CGITIPEGLE KDQKLPELLI TPSTKGVLTG
     LEGVPEADDV NVSRSDIERH VDGFNFSSLS DIDLYEKLLK EGFDVISDAL AEHDQIFVDT
     KFEFGYVNDA AGNEKLIYMD EVGTPDSSRI WDGSSHRDGK IIEQSKEGFR QWLLNHFPDA
     DILLNKNRME ERFALAKDNK LPESVMMDIS NTYVGIAEKV IGEKLHISEN PKQEIIDILR
     SEYQLIV