ID M0FKR9_9EURY Unreviewed; 125 AA. AC M0FKR9; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 26-NOV-2014, entry version 11. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021}; DE Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01021}; DE EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01021}; GN Name=hisI {ECO:0000256|HAMAP-Rule:MF_01021}; GN ORFNames=C459_17321 {ECO:0000313|EMBL:ELZ60500.1}; OS Haloferax sp. ATCC BAA-645. OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; Haloferax. OX NCBI_TaxID=1227463 {ECO:0000313|EMBL:ELZ60500.1}; RN [1] {ECO:0000313|EMBL:ELZ60500.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC BAA-645 {ECO:0000313|EMBL:ELZ60500.1}; RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., RA Darling A., Eisen J.A., Facciotti M.T.; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of CC phosphoribosyl-AMP. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01021}. CC -!- COFACTOR: CC Note=Binds 1 magnesium ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01021}; CC -!- COFACTOR: CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01021}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021}. CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP- CC Rule:MF_01021}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ELZ60500.1}. 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; AOLE01000037; ELZ60500.1; -; Genomic_DNA. DR EnsemblBacteria; ELZ60500; ELZ60500; C459_17321. 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 {ECO:0000256|HAMAP-Rule:MF_01021}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01021, KW ECO:0000313|EMBL:ELZ60500.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01021}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01021}. FT METAL 79 79 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01021}. FT METAL 80 80 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01021}. FT METAL 81 81 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01021}. FT METAL 83 83 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01021}. FT METAL 96 96 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01021}. FT METAL 103 103 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01021}. SQ SEQUENCE 125 AA; 13870 MW; 4BFCA52910B547C6 CRC64; MADESVDIEL DFGDDGLVPA VAQDADTDEV LMLAYASPDA VAATRETGLA HYYSRSRDEL WKKGGTSGHI QEVREIRVDC DRDALLYRVE QEGGACHTGY RSCFSRTIDG EEVGEKVYDP DEVYD //