ID   HIS3_BACHK              Reviewed;         101 AA.
AC   Q6HLE2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE            Short=PRA-CH;
DE            EC=3.5.4.19;
GN   Name=hisI; OrderedLocusNames=BT9727_1295;
OS   Bacillus thuringiensis subsp. konkukian.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180856;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
CC   -!- CATALYTIC ACTIVITY: 1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5-
CC       phosphoribosyl)-5-((5-
CC       phosphoribosylamino)methylideneamino)imidazole-4-carboxamide.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PRA-CH family.
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DR   EMBL; AE017355; AAT59423.1; -; Genomic_DNA.
DR   RefSeq; YP_035629.1; -.
DR   GeneID; 2854182; -.
DR   GenomeReviews; AE017355_GR; BT9727_1295.
DR   KEGG; btk:BT9727_1295; -.
DR   HOGENOM; Q6HLE2; -.
DR   OMA; Q6HLE2; LWLKGES.
DR   BioCyc; BTHU281309:BT9727_1295-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01021; -; 1.
DR   InterPro; IPR002496; PRA_CycHdrlase.
DR   Pfam; PF01502; PRA-CH; 1.
DR   ProDom; PD002610; PRA_cyclohydro; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase.
FT   CHAIN         1    101       Phosphoribosyl-AMP cyclohydrolase.
FT                                /FTId=PRO_0000229810.
SQ   SEQUENCE   101 AA;  11607 MW;  FDA6E19DE50A01F1 CRC64;
     MKPNFSKGLL PAVVIEEGTK EVLMLAYMNE EAYEKTLKTK RTWFYSRSRR SLWNKGETSG
     HVQHVQSLYL DCDQDAIVVV VKQVGPACHT GEKTCFHYKI I
//