ID   PUR7_CLOP1              Reviewed;         235 AA.
AC   Q0TTB4;
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=CPF_0673;
OS   Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
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; CP000246; ABG83396.1; -; Genomic_DNA.
DR   RefSeq; YP_695126.1; -.
DR   GeneID; 4203660; -.
DR   GenomeReviews; CP000246_GR; CPF_0673.
DR   KEGG; cpf:CPF_0673; -.
DR   TIGR; CPF_0673; -.
DR   HOGENOM; Q0TTB4; -.
DR   OMA; Q0TTB4; 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_1000018692.
SQ   SEQUENCE   235 AA;  27003 MW;  3A41A843F0D61F96 CRC64;
     MVNQLEMLYE GKAKKIYATD KEDMVIVHYK DDATAFNGEK KAQIESKGVL NNEITSLIFE
     MLNKEGIKTH FVEKLNDRDQ LCKKVEIVPL EVIVRNVAAG SMAKRLGLEE GYELKTTVFE
     LSYKDDSLGD PLINDYHAVG IGATTFEELN KIYEITAKVN EILKEAFKKQ NINLIDFKLE
     FGRYNGEILL ADEISPDTCR FWDATTGEKM DKDRFRRDMG NVINGYREVL NRLRN
//