ID   PUR9_CLOPS              Reviewed;         501 AA.
AC   Q0SV48;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Bifunctional purine biosynthesis protein purH;
DE   Includes:
DE     RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE              EC=2.1.2.3;
DE     AltName: Full=AICAR transformylase;
DE   Includes:
DE     RecName: Full=IMP cyclohydrolase;
DE              EC=3.5.4.10;
DE     AltName: Full=Inosinicase;
DE     AltName: Full=IMP synthetase;
DE     AltName: Full=ATIC;
GN   Name=purH; OrderedLocusNames=CPR_0675;
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: 10-formyltetrahydrofolate + 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
CC   -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamide.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl
CC       THF route): step 1/1.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC       carboxamide: step 1/1.
CC   -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC       region (By similarity).
CC   -!- SIMILARITY: Belongs to the purH family.
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DR   EMBL; CP000312; ABG87320.1; -; Genomic_DNA.
DR   RefSeq; YP_698002.1; -.
DR   GeneID; 4206513; -.
DR   GenomeReviews; CP000312_GR; CPR_0675.
DR   KEGG; cpr:CPR_0675; -.
DR   TIGR; CPR_0675; -.
DR   HOGENOM; Q0SV48; -.
DR   OMA; Q0SV48; VVKHVKS.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:HAMAP.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide for...; IEA:HAMAP.
DR   GO; GO:0006188; P:IMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00139; -; 1.
DR   InterPro; IPR002695; AICARFT_IMPCHas.
DR   InterPro; IPR013982; AICARFT_IMPCHas_formly.
DR   InterPro; IPR011607; MGS.
DR   PANTHER; PTHR11692; AICARFT_IMPCHas; 1.
DR   Pfam; PF01808; AICARFT_IMPCHas; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR   SMART; SM00798; AICARFT_IMPCHas; 1.
DR   TIGRFAMs; TIGR00355; purH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Multifunctional enzyme;
KW   Purine biosynthesis; Transferase.
FT   CHAIN         1    501       Bifunctional purine biosynthesis protein
FT                                purH.
FT                                /FTId=PRO_1000018881.
SQ   SEQUENCE   501 AA;  56108 MW;  BE889F267E4A911D CRC64;
     MKKRALISVF DKDGVLELAK FLRDRDVEII SSGGTYKYLK ENNIEVKEIS EITDFPEMLD
     GRVKTLHPLV HAGILAIRDN KEHMKTLEKR EINTIDYVVV NLYPFFEKVR ENLSFEEKVE
     FIDIGGPTML RAAAKNFKDV VVLSDKKDYE KVMNEIKENN CVSFKLRKTL AGKVFNLMSA
     YDAAISNFLL EGEEEYPEYL SVSYKKIQDL RYGENPHQGA AYYSSTEFDG AMNSFEILNG
     KALSYNNIKD LDIAWKVACE FEETACCALK HNTPCGVAVG ENSKEVYLKA YDADPVSIFG
     GIVAINRKID KATAEEMVKI FLEVVAAPDF DEDALEVLRT KKNLRVIKCK NTPQAKNYMV
     TVDGGILVQG EDNKLANEYK VVTKKEPTEM ELRDMIFGMK VVKYVKSNAI VVVKDGVATG
     IGGGQVNRIW ATKEALERGK GGAVLASDAF FPFRDCVDEA AKNGIKAIIQ PGGSIRDEES
     VEACNEHGIS MVFTGVRHFK H
//