ID   PUR7_CLOPS              Reviewed;         235 AA.
AC   Q0SV52;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE            EC=6.3.2.6;
DE   AltName: Full=SAICAR synthetase;
GN   Name=purC; OrderedLocusNames=CPR_0671;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate +
CC       (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
CC       carboxamido)succinate.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 4/5.
CC   -!- SIMILARITY: Belongs to the SAICAR synthetase family.
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DR   EMBL; CP000312; ABG86858.1; -; Genomic_DNA.
DR   RefSeq; YP_697998.1; -.
DR   GeneID; 4205558; -.
DR   GenomeReviews; CP000312_GR; CPR_0671.
DR   KEGG; cpr:CPR_0671; -.
DR   TIGR; CPR_0671; -.
DR   HOGENOM; Q0SV52; -.
DR   OMA; Q0SV52; TAFNAQK.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxam...; IEA:HAMAP.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00137; -; 1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001636; SAICAR_synt.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   PANTHER; PTHR11609; SAICAR_synt; 1.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   ProDom; PD003043; 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; Complete proteome; Ligase; Nucleotide-binding;
KW   Purine biosynthesis.
FT   CHAIN         1    235       Phosphoribosylaminoimidazole-
FT                                succinocarboxamide synthase.
FT                                /FTId=PRO_1000018693.
SQ   SEQUENCE   235 AA;  27044 MW;  B1D1AE9E460BB167 CRC64;
     MVNQLEMLYE GKAKKIYATD KEDMVIVHYK DDATAFNGEK KAQIESKGVL NNEITSLIFE
     MLNKEGIKTH FVEKLNDRDQ LCKKVEIVPL EVIVRNVAAG SMAKRLGLEE GYELKTTVFE
     LSYKDDSLGD PLINDYHAVG IGATTFEELN KIYEITAKVN EILKEAFKKQ NINLIDFKLE
     FGRYKGEILL ADEISPDTCR FWDAKTGEKM DKDRFRRDMG NVINGYREVL NRLRN
//