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PUR7_VIBVY
ID   PUR7_VIBVY              Reviewed;         367 AA.
AC   Q7MLF9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 108.
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=VV1468;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC94232.1; -; Genomic_DNA.
DR   RefSeq; WP_011080630.1; NC_005139.1.
DR   AlphaFoldDB; Q7MLF9; -.
DR   SMR; Q7MLF9; -.
DR   STRING; 672.VV93_v1c13770; -.
DR   EnsemblBacteria; BAC94232; BAC94232; BAC94232.
DR   KEGG; vvy:VV1468; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_064197_0_0_6; -.
DR   OMA; QKARPVM; -.
DR   OrthoDB; 1345271at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000002675; 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;
KW   Reference proteome.
FT   CHAIN           1..367
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_0000100898"
SQ   SEQUENCE   367 AA;  40817 MW;  14EF20EB7B9BFE9E CRC64;
     MSLADQVLAV NDDLPIRTDK PVHSGKVRSV YWLTEEDSAR LIKEKGYNVA PDAPLAIMVI
     SDRISAFDCI WHGEHGLNGV PGKGAALNAI SNHWFGLFKE NGLADSHILD IPHPFVWIVQ
     KAKPVKIEAI CRKYITGSMW RAYEKGEREF CGIQLPEGLE KDKALPDLLM TPSTKGILKG
     IPGVPEADDV NITRQNIADN FAAFNFSSAD DIALYEKLLK DGFGVISEAL ANVGQIFVDT
     KFEFGYVTDA AGNEKLIYMD EVGTPDSSRI WDAQEYQAGK IVENSKEGFR QFLLNYFPDP
     DILLNKDRMP EREALARDNE LPEEALMAVS RTYINIAEKI TGSAIVLSDN PKQEIIDILG
     REYGLID
 
 
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