ID HIS3_BIFAA Reviewed; 135 AA. AC A1A1I6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 16-JUN-2009, entry version 20. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase; DE Short=PRA-CH; DE EC=3.5.4.19; GN Name=hisI; OrderedLocusNames=BAD_0788; 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)-AMP + H(2)O = 1-(5- CC phosphoribosyl)-5-((5- CC phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the PRA-CH 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; BAF39569.1; -; Genomic_DNA. DR RefSeq; YP_909651.1; -. DR GeneID; 4556177; -. DR GenomeReviews; AP009256_GR; BAD_0788. DR KEGG; bad:BAD_0788; -. DR NMPDR; fig|1680.3.peg.1372; -. DR OMA; A1A1I6; LWLKGES. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01021; -; 1. DR InterPro; IPR002496; PRA_CycHdrlase. DR Pfam; PF01502; PRA-CH; 1. DR ProDom; PD002610; PRA_cyclohydro; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase. FT CHAIN 1 135 Phosphoribosyl-AMP cyclohydrolase. FT /FTId=PRO_1000063389. SQ SEQUENCE 135 AA; 15208 MW; 494426749E950B48 CRC64; MTNEAYDNTT TLDPRIAQRL KHDDKGLVAA VIQQFDTKEV LMVGYMNDEA IRRTLTTGRV TFWSRSRQEY WRKGDTSGHA QYVKSFALDC DGDAILVEVD QVGAACHTGK RSCFEEGGQL PVVVGHRTKE QEGQR //