ID   PUR7_BACTN              Reviewed;         314 AA.
AC   Q8A004;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=BT_4217;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(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; AE015928; AAO79322.1; -; Genomic_DNA.
DR   RefSeq; NP_813128.1; NC_004663.1.
DR   RefSeq; WP_008759891.1; NZ_UYXG01000012.1.
DR   AlphaFoldDB; Q8A004; -.
DR   SMR; Q8A004; -.
DR   STRING; 226186.BT_4217; -.
DR   PaxDb; Q8A004; -.
DR   PRIDE; Q8A004; -.
DR   EnsemblBacteria; AAO79322; AAO79322; BT_4217.
DR   GeneID; 60925390; -.
DR   KEGG; bth:BT_4217; -.
DR   PATRIC; fig|226186.12.peg.4285; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_045637_0_1_10; -.
DR   InParanoid; Q8A004; -.
DR   OMA; TKFEFGF; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
DR   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..314
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_0000100802"
SQ   SEQUENCE   314 AA;  35766 MW;  4D8D0095800BE405 CRC64;
     MKALTKTDFN FPGQKSVYHG KVRDVYNING EKLVMVATDR ISAFDVVLPE GIPYKGQMLN
     QIAAKFLDAT TDICPNWKMA TPDPMVTVGV LCEGFPVEMI VRGYLCGSAW RTYKSGVREI
     CGVKLPDGMR ENEKFPEPIV TPTTKAEMGL HDEDISKEEI LKQGLATPEE YETLEKYTLA
     LFKRGTEIAA ERGLILVDTK YEFGKHNGTI YLMDEIHTPD SSRYFYSDGY QERFEKGEPQ
     KQLSKEFVRE WLMENGFQGK DGQKVPEMTP AIVQSISDRY IELFENITGE KFVKEDTSNI
     AERIEKNVMN FLSK