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 29-OCT-2014, entry version 52. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01021}; DE Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01021}; DE EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01021}; GN Name=hisI {ECO:0000255|HAMAP-Rule:MF_01021}; GN 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 -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of CC phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021}. 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 {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- COFACTOR: Binds 1 magnesium ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01021}. CC -!- COFACTOR: Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01021}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000255|HAMAP- CC Rule:MF_01021}. 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; HEPGIAC; -. DR OrthoDB; EOG6PGKB6; -. DR BioCyc; MSP156889:GH36-3199-MONOMER; -. DR UniPathway; UPA00031; UER00008. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; Magnesium; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 129 Phosphoribosyl-AMP cyclohydrolase. FT /FTId=PRO_0000319695. FT METAL 79 79 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 80 80 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. FT METAL 81 81 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 83 83 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 96 96 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. FT METAL 103 103 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. SQ SEQUENCE 129 AA; 14620 MW; CBF9C967E72C32AD CRC64; MEKLPDLATL KYNEQGLIPA IAQQYDTGEV LMMAWMNQTS LAETLSTGVA CYWSRSRNRF WRKGESSGQV QTVKAVRLDC DKDTLLLLVD QQGVACHTGR HNCFYLEAQD GSWKTITDPE IDPEELYGK //