ID HIS2_ACICJ Reviewed; 133 AA. AC A5FYE6; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 16-JUN-2009, entry version 16. DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase; DE Short=PRA-PH; DE EC=3.6.1.31; GN Name=hisE; OrderedLocusNames=Acry_1418; OS Acidiphilium cryptum (strain JF-5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Acidiphilium. OX NCBI_TaxID=349163; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T., RA Richardson P.; RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000697; ABQ30628.1; -; Genomic_DNA. DR RefSeq; YP_001234547.1; -. DR GeneID; 5161220; -. DR GenomeReviews; CP000697_GR; Acry_1418. DR KEGG; acr:Acry_1418; -. DR OMA; A5FYE6; LSGHAEK. 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 1 133 Phosphoribosyl-ATP pyrophosphatase. FT /FTId=PRO_0000319634. SQ SEQUENCE 133 AA; 14395 MW; FF66D6357A1753F5 CRC64; MGAASHPPVP LLNPAAPNAQ VLDRLWSTIL ARKAADPLVS HSARLLSRGV NKVAQKFGEE SVECLIEAVA GNRTALIAES ADVLYHLLVM WVAAGVRPED VWLELQRREG ISGITEKASR PMLLSIAETR KIP //