ID HIS2_BURXL Reviewed; 131 AA. AC Q13TR2; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-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=Bxeno_A3989; ORFNames=Bxe_A0406; OS Burkholderia xenovorans (strain LB400). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., RA Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., RA Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M., RA Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., RA Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp RT genome shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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. 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; CP000270; ABE32527.1; -; Genomic_DNA. DR RefSeq; YP_560579.1; -. DR GeneID; 4006012; -. DR GenomeReviews; CP000270_GR; Bxeno_A3989. DR KEGG; bxe:Bxe_A0406; -. DR HOGENOM; Q13TR2; -. DR OMA; Q13TR2; 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 1 131 Phosphoribosyl-ATP pyrophosphatase. FT /FTId=PRO_0000319644. SQ SEQUENCE 131 AA; 14218 MW; 05E50342783EC054 CRC64; MTQSTQTTPS NAASTTDTLL RLAAIIDSRK GGDPEVSYVS RLFHKGDDAV LKKIGEEATE VVLAAKDARH GGAPKALVGE VADLWFHCLV MLSHFDLSPA DVLAELERRE GMSGIEEKAL RKSRDREQNG D //