ID HIS2_BIFAA Reviewed; 87 AA. AC A1A1J2; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. 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=BAD_0794; OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083). OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=367928; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., RA Hirai S., Tanaka K., Watanabe K.; RT "Bifidobacterium adolescentis complete genome sequence."; RL Submitted (DEC-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; AP009256; BAF39575.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_909657.1; -. DR GeneID; 4556154; -. DR GenomeReviews; AP009256_GR; BAD_0794. DR KEGG; bad:BAD_0794; -. DR NMPDR; fig|1680.3.peg.1378; -. 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_0000319641. SQ SEQUENCE 87 AA; 9756 MW; 58400EBCA77E4308 CRC64; MKTFESLFAE LSEKAATKQA GSLTVDELAK GTHFIGKKIV EEAGETWIAA EYEGADRTAE EMSQLIYHLQ VMMIDRGITL EDIYKNL //