ID   HIS3_BACAH              Reviewed;         101 AA.
AC   A0RBM3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE            Short=PRA-CH;
DE            EC=3.5.4.19;
GN   Name=hisI; OrderedLocusNames=BALH_1266;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N.,
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., Green L.D., Han C.S., Hill K.K., Hitchcock P.,
RA   Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S.,
RA   Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O.,
RA   Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
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; CP000485; ABK84616.1; -; Genomic_DNA.
DR   RefSeq; YP_894123.1; -.
DR   GeneID; 4546879; -.
DR   GenomeReviews; CP000485_GR; BALH_1266.
DR   KEGG; btl:BALH_1266; -.
DR   NMPDR; fig|412694.5.peg.1279; -.
DR   OMA; A0RBM3; LWLKGES.
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_1000063388.
SQ   SEQUENCE   101 AA;  11623 MW;  FDB5C0AFE50A01F1 CRC64;
     MKPNFSKGLL PAVVIEEGTK EVLMLAYMNE EAYEKTLKTK RTWFYSRSRR SLWNKGETSG
     HVQHVQSLYL DCDQDSIVVV VKQVGPACHT GEKTCFHYKI I
//