ID   PUR7_AERS4              Reviewed;         367 AA.
AC   A4SR47;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=ASA_3394;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(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; CP000644; ABO91369.1; -; Genomic_DNA.
DR   RefSeq; WP_005311616.1; NC_009348.1.
DR   AlphaFoldDB; A4SR47; -.
DR   SMR; A4SR47; -.
DR   STRING; 382245.ASA_3394; -.
DR   EnsemblBacteria; ABO91369; ABO91369; ASA_3394.
DR   KEGG; asa:ASA_3394; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_064197_0_0_6; -.
DR   OMA; QKARPVM; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000000225; 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_1000117821"
SQ   SEQUENCE   367 AA;  41035 MW;  F1B3CF5651339453 CRC64;
     MSLADQVLAV NDDLPIRTDK PVHSGKVRSV YWLTPEDSAR LIKEKGYDVP ADAPLALMVI
     SDRISAFDCI WQGVDGLNGV PGKGAALNAI SSHWFKLFKE KGLADSHILD IPHPFVWIVQ
     KARPVMIEAI ARQYITGSMW RAYKDGEREF CGITLPEGLK KDQKLPEILI TPSTKGVLTG
     LDGVPEADDV NVSRADIERH YQGFNFSKPA DIDRYEVLLK EGFNVISDAL ASLDQIFVDT
     KFEFGYVQDA AGNEKLIYMD EVGTPDSSRI WDGAALRDGQ IVEKSKEGFR QWLLNHFPDP
     DILLNKNRMP ERFALAKGNK LPTEVMMDIS NTYVGIAEKI IGHPLVRSAN PKQEIIEVLR
     DQYGLID