ID   PUR7_VIBC1              Reviewed;         367 AA.
AC   A7MVN0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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};
GN   OrderedLocusNames=VIBHAR_02039;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-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; CP000789; ABU71004.1; -; Genomic_DNA.
DR   RefSeq; WP_012127782.1; NC_022269.1.
DR   AlphaFoldDB; A7MVN0; -.
DR   SMR; A7MVN0; -.
DR   EnsemblBacteria; ABU71004; ABU71004; VIBHAR_02039.
DR   KEGG; vha:VIBHAR_02039; -.
DR   PATRIC; fig|338187.25.peg.650; -.
DR   OMA; QKARPVM; -.
DR   OrthoDB; 1345271at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000008152; Chromosome I.
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   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   TIGRFAMs; TIGR02735; purC_vibrio; 1.
DR   PROSITE; PS01057; SAICAR_SYNTHETASE_1; 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_1000117862"
SQ   SEQUENCE   367 AA;  41074 MW;  3835F075FE8296A5 CRC64;
     MSLANQVLAV NDDLPIRTHK PVHSGKVRSV YWLTEEDSAR LIKEKGYDVA PDAPLAIMVI
     SDRISAFDCI WHGEGGLKGV PGKGAALNAI SNHWFKLFKD NGLADSHILD IPHPFVWIVQ
     KAKPVKIEAI CRKYITGSMW RAYANGEREF CGIELPEGLE KDKALPELLM TPSTKGILKG
     IPGVPEADDV NITRQNIVDN FEAFNFSNAK DIAQYEKLLK EGFNVISSAL EAIDQTFVDT
     KFEFGYVHDA AGNEKLIYMD EVGTPDSSRI WDTKEYQAGN IVENSKEGFR QFLLSHFPDP
     DILLNKERMP EREALARDNE LPVESLMDIS RTYIGIAEKI TGQPIKLSND PKAEIIEILS
     KEYGLID