ID   PUR7_GEOSM              Reviewed;         296 AA.
AC   C6E6C1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=GM21_1708;
OS   Geobacter sp. (strain M21).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) 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; CP001661; ACT17762.1; -; Genomic_DNA.
DR   RefSeq; WP_015837009.1; NC_012918.1.
DR   AlphaFoldDB; C6E6C1; -.
DR   SMR; C6E6C1; -.
DR   STRING; 443144.GM21_1708; -.
DR   EnsemblBacteria; ACT17762; ACT17762; GM21_1708.
DR   KEGG; gem:GM21_1708; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_045637_0_0_7; -.
DR   OMA; TKFEFGF; -.
DR   UniPathway; UPA00074; UER00131.
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; IPR001636; SAICAR_synth.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   TIGRFAMs; TIGR00081; purC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..296
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_1000203231"
SQ   SEQUENCE   296 AA;  33114 MW;  F408D667F1A31A66 CRC64;
     MTTPVLNTDF PGLKLAARGK VRDIYDLGET LLIVTTDRIS AFDVIMNEGI PHKGYVLTQI
     SAYWFRQMEG IIKNHIISTD VADFPKECQP YADVLAGRSM WVKKAQPLAA ECIVRGYISG
     SGWKDYQSTG AICGIKLPEG LKESDRLPQP IFTPSTKAEL GTHDENISFE EMCRICGTEI
     STKVRDVTLA IYEKARDIAD QKGIIIADTK FEYGIYEGEL IIIDECMTPD SSRFWPKDSY
     KPGGPQPSFD KQFLRDYLET LDWGKTAPAP PLPEEIVRKT GEKYMEALVK LTGKGI