ID HIS3_MAGSM Reviewed; 129 AA. AC A0LCF4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 19-FEB-2014, entry version 48. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase; DE Short=PRA-CH; DE EC=3.5.4.19; GN Name=hisI; OrderedLocusNames=Mmc1_3157; OS Magnetococcus sp. (strain MC-1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC-1; RG US DOE Joint Genome Institute; 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., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of Magnetococcus sp. MC-1."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- CC ribosylamino)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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000471; ABK45647.1; -; Genomic_DNA. DR RefSeq; YP_867053.1; NC_008576.1. DR ProteinModelPortal; A0LCF4; -. DR STRING; 156889.Mmc1_3157; -. DR EnsemblBacteria; ABK45647; ABK45647; Mmc1_3157. DR GeneID; 4483260; -. DR KEGG; mgm:Mmc1_3157; -. DR PATRIC; 22432959; VBIMagSp23654_3210. DR eggNOG; COG0139; -. DR HOGENOM; HOG000277504; -. DR KO; K01496; -. DR OMA; GACHVGY; -. DR OrthoDB; EOG6PGKB6; -. DR BioCyc; MSP156889:GH36-3199-MONOMER; -. DR UniPathway; UPA00031; UER00008. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01021; HisI; 1. DR InterPro; IPR026660; PRA-CH. DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom. DR Pfam; PF01502; PRA-CH; 1. DR ProDom; PD002610; PRA_CycHdrlase; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase. FT CHAIN 1 129 Phosphoribosyl-AMP cyclohydrolase. FT /FTId=PRO_0000319695. SQ SEQUENCE 129 AA; 14620 MW; CBF9C967E72C32AD CRC64; MEKLPDLATL KYNEQGLIPA IAQQYDTGEV LMMAWMNQTS LAETLSTGVA CYWSRSRNRF WRKGESSGQV QTVKAVRLDC DKDTLLLLVD QQGVACHTGR HNCFYLEAQD GSWKTITDPE IDPEELYGK //