ID   PUR7_RHOOB              Reviewed;         294 AA.
AC   C1AT85;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=ROP_49020;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-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; AP011115; BAH53149.1; -; Genomic_DNA.
DR   RefSeq; WP_015888661.1; NC_012522.1.
DR   AlphaFoldDB; C1AT85; -.
DR   SMR; C1AT85; -.
DR   STRING; 632772.ROP_49020; -.
DR   EnsemblBacteria; BAH53149; BAH53149; ROP_49020.
DR   KEGG; rop:ROP_49020; -.
DR   PATRIC; fig|632772.20.peg.5122; -.
DR   HOGENOM; CLU_045637_0_0_11; -.
DR   OMA; TKFEFGF; -.
DR   OrthoDB; 1345271at2; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000002212; 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; 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.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..294
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_1000122925"
SQ   SEQUENCE   294 AA;  32059 MW;  37704C2D7136D37F CRC64;
     MRPSLDSYAH LAGGKVRDLY TIDDEHLLLV ASDRISAYDH VLSTPIPDKG RVLTAMSVFF
     FGVLGGNNHL AGEPDDSRIP EEVLGRALVV RKLNMVPVEC VARGYLTGSG LIDYNETGAV
     CGVALPEGLV EASQLPDPIF TPARKAELGE HDENISFEAV VEKVGQDLAV KLRDDTLDVY
     GRASNFAADR GIILADTKLE FGLDAQNNLI LADEVLTPDS SRYWPADGYE AGKVQPSFDK
     QFVRNWLTGP ESGWDRASDT PPPPLPAEIV EATRARYIEA YERISGLSFA DWVG