ID   HIS2_CLAM3              Reviewed;          87 AA.
AC   A5CRW4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 15.
DE   RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE            Short=PRA-PH;
DE            EC=3.6.1.31;
GN   Name=hisE; OrderedLocusNames=CMM_1771;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O.,
RA   Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S.,
RA   Rueckert C., Schneiker S., Zellermann E.-M., Puehler A.,
RA   Eichenlaub R., Kaiser O., Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island
RT   involved in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN01827.1; -; Genomic_DNA.
DR   RefSeq; YP_001222514.1; -.
DR   GeneID; 5174010; -.
DR   GenomeReviews; AM711867_GR; CMM_1771.
DR   KEGG; cmi:CMM_1771; -.
DR   OMA; A5CRW4; VWMAAEY.
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     87       Phosphoribosyl-ATP pyrophosphatase.
FT                                /FTId=PRO_1000063334.
SQ   SEQUENCE   87 AA;  9634 MW;  E9B5634F35318D91 CRC64;
     MKTFDDLFGE LTRIAAERPE GSGTVRELDG GVHAIGKKVV EEAAEVWMAA EHESDDRAAE
     EISQLLYHVQ VMMIARGLTL EDVGRHL
//