ID   HIS2_BACHK              Reviewed;         107 AA.
AC   Q6HLE1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=BT9727_1296;
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)-ATP + H(2)O = 1-(5-
CC       phosphoribosyl)-AMP + diphosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PRA-PH family.
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DR   EMBL; AE017355; AAT59424.1; -; Genomic_DNA.
DR   RefSeq; YP_035630.1; -.
DR   SMR; Q6HLE1; 4-95.
DR   GeneID; 2856158; -.
DR   GenomeReviews; AE017355_GR; BT9727_1296.
DR   KEGG; btk:BT9727_1296; -.
DR   NMPDR; fig|281309.1.peg.1270; -.
DR   HOGENOM; Q6HLE1; -.
DR   OMA; Q6HLE1; GADPDSS.
DR   BioCyc; BTHU281309:BT9727_1296-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01020; -; 1.
DR   InterPro; IPR008179; PRib-ATP_pyrophosphohydrolase.
DR   Pfam; PF01503; PRA-PH; 1.
DR   ProDom; PD002611; Pra_PH/CH; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Nucleotide-binding.
FT   CHAIN         1    107       Phosphoribosyl-ATP pyrophosphatase.
FT                                /FTId=PRO_0000230167.
SQ   SEQUENCE   107 AA;  12466 MW;  38F03898C7351E2D CRC64;
     MRNAFTLLFE TIEERKNNPL PESYTNYLFS KGEDKILKKI GEECSEVIIA SKNNDNEELV
     KEMVDVLYHC FVLLAEKNIP LKDIMEEVTE RNGKLSRVGD RREIDTL
//