ID   PUR5_CLOP1              Reviewed;         333 AA.
AC   Q0TTB2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE            EC=6.3.3.1;
DE   AltName: Full=AIRS;
DE   AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
DE   AltName: Full=AIR synthase;
GN   Name=purM; OrderedLocusNames=CPF_0675;
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 + 2-(formamido)-N(1)-(5-phospho-D-
CC       ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole.
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 2/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the AIR synthase family.
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DR   EMBL; CP000246; ABG84389.1; -; Genomic_DNA.
DR   RefSeq; YP_695128.1; -.
DR   GeneID; 4201607; -.
DR   GenomeReviews; CP000246_GR; CPF_0675.
DR   KEGG; cpf:CPF_0675; -.
DR   TIGR; CPF_0675; -.
DR   HOGENOM; Q0TTB2; -.
DR   OMA; Q0TTB2; CGKLDPE.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-lig...; IEA:HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00741; -; 1.
DR   InterPro; IPR000728; AIR_synth.
DR   InterPro; IPR010918; AIR_synth_C.
DR   InterPro; IPR004733; PurM_cligase.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   TIGRFAMs; TIGR00878; purM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Purine biosynthesis.
FT   CHAIN         1    333       Phosphoribosylformylglycinamidine cyclo-
FT                                ligase.
FT                                /FTId=PRO_0000258347.
SQ   SEQUENCE   333 AA;  36440 MW;  78B8A6FCA8B44275 CRC64;
     MLTYKEAGVN IEEGYRSVKL IKEYAKKTMS EYVLNGLGSF AGMVELPEGY KKPVLVSGTD
     GVGTKLDIAC KKRKFDTVGI DCVAMCVNDI LCHGAKPLFF LDYIACGKLE AEVSSDLVKG
     VAEGCIESQC SLIGGETAEM PGMYKEGDYD IAGFAVGIVD KDKIINGKDI KSGDKLIGIA
     SSGVHSNGYS LIRKVFKNLD EDFNGKAIWE ELLTPTKIYV KPVLSLLEKF NIKGMAHVTG
     GGFYENLPRM LSKEGLSIVI NKNSYEIPEI FKKLMELGVK EEEMYNTFNM GIGFVLCVEE
     DEVEEVLKEL SKQGEKAFEI GYINAGGEGV CIK
//