ID HIS2_BURCM Reviewed; 121 AA. AC Q0BIW2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase; DE Short=PRA-PH; DE EC=3.6.1.31; GN Name=hisE; OrderedLocusNames=Bamb_0351; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; 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., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) 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; CP000440; ABI85911.1; -; Genomic_DNA. DR RefSeq; YP_772245.1; -. DR GeneID; 4309244; -. DR GenomeReviews; CP000440_GR; Bamb_0351. DR KEGG; bam:Bamb_0351; -. DR NMPDR; fig|339670.3.peg.5467; -. DR OMA; Q0BIW2; 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 1 121 Phosphoribosyl-ATP pyrophosphatase. FT /FTId=PRO_1000063326. SQ SEQUENCE 121 AA; 13274 MW; B84C1B53F98826F8 CRC64; MTQSTEDTLL RLAAVIDSRK GGDPDQSYVS RLFHKGDDAV LKKIGEEATE VVLAAKDVRQ GGAPTALVGE VADLWFHCLV MLSHFDLSPA DVIGELERRE GLSGIEEKAL RKRREREENG G //