ID   PUR7_THEYD              Reviewed;         292 AA.
AC   B5YFN3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=THEYE_A1265;
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) 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; CP001147; ACI20723.1; -; Genomic_DNA.
DR   RefSeq; WP_012545457.1; NC_011296.1.
DR   RefSeq; YP_002249081.1; NC_011296.1.
DR   AlphaFoldDB; B5YFN3; -.
DR   SMR; B5YFN3; -.
DR   STRING; 289376.THEYE_A1265; -.
DR   EnsemblBacteria; ACI20723; ACI20723; THEYE_A1265.
DR   KEGG; tye:THEYE_A1265; -.
DR   PATRIC; fig|289376.4.peg.1236; -.
DR   eggNOG; COG0152; Bacteria.
DR   HOGENOM; CLU_045637_0_2_0; -.
DR   InParanoid; B5YFN3; -.
DR   OMA; TKFEFGF; -.
DR   OrthoDB; 1345271at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000000718; 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; IPR001636; SAICAR_synth.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   TIGRFAMs; TIGR00081; purC; 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..292
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_1000096025"
SQ   SEQUENCE   292 AA;  33198 MW;  05D4339D7B10E859 CRC64;
     MKNVVLETNL KGVKLLRRGK VRDIYEIEDY LLIVATDRVS AFDVVLPTGI PEKGKILTQI
     SLFWFDKVKD IVENHLVSAN ADEFPEPLPA YKEILEGRSM LVKKAKPLPV ECIVRGYLSG
     SGWKDYQKTG MICGIKLPEG LVESAKLPEP VFTPSTKAEQ GHDINISFEE TIQILGEETA
     QKVKELSLSI YKKAAQIAEK KGIIIADTKM EFGFYNGKLI LIDELLTPDS SRFWSLENYR
     IGYPQDSYDK QIVRDYLLSI KWDKKPPAPQ LPEDIVNKTA ERYKEIFRIL TS