ID A0A4U0QJE9_9RHOB Unreviewed; 118 AA. AC A0A4U0QJE9; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 2. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976554}; DE Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01021}; DE EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976537}; GN Name=hisI {ECO:0000256|HAMAP-Rule:MF_01021, GN ECO:0000313|EMBL:TJZ81835.1}; GN ORFNames=FA740_16165 {ECO:0000313|EMBL:TJZ81835.1}; OS Paracoccus hibiscisoli. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=2023261 {ECO:0000313|EMBL:TJZ81835.1}; RN [1] {ECO:0000313|EMBL:TJZ81835.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCTCC AB2016182 {ECO:0000313|EMBL:TJZ81835.1}; RA Li J.; RL Submitted (APR-2019) 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 ECO:0000256|SAAS:SAAS00976573}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho- CC beta-D-ribosyl)-5-[(5-phospho-beta-D- CC ribosylamino)methylideneamino]imidazole-4-carboxamide; CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435, CC ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01021, ECO:0000256|SAAS:SAAS01115149}; 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, ECO:0000256|SAAS:SAAS00976563}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01021, CC ECO:0000256|SAAS:SAAS00976534}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021, CC ECO:0000256|SAAS:SAAS00976539}. CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000256|HAMAP- CC Rule:MF_01021, ECO:0000256|SAAS:SAAS00976567}. 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:TJZ81835.1}. 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; SUNH01000027; TJZ81835.1; -; Genomic_DNA. DR UniPathway; UPA00031; UER00008. DR Gene3D; 3.10.20.400; -; 1. DR HAMAP; MF_01021; HisI; 1. DR InterPro; IPR026660; PRA-CH. DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom. DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf. DR Pfam; PF01502; PRA-CH; 1. DR SUPFAM; SSF141734; SSF141734; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021, KW ECO:0000256|SAAS:SAAS00976560}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01021, KW ECO:0000256|SAAS:SAAS00976532}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01021, KW ECO:0000256|SAAS:SAAS00976556}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01021, KW ECO:0000256|SAAS:SAAS00976548, ECO:0000313|EMBL:TJZ81835.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01021, KW ECO:0000256|SAAS:SAAS00976550}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01021, KW ECO:0000256|SAAS:SAAS00976576}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01021, ECO:0000256|SAAS:SAAS00976542}. FT DOMAIN 29 102 PRA-CH. {ECO:0000259|Pfam:PF01502}. FT METAL 76 76 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01021}. FT METAL 77 77 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01021}. FT METAL 78 78 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01021}. FT METAL 80 80 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01021}. FT METAL 93 93 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01021}. FT METAL 100 100 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01021}. SQ SEQUENCE 118 AA; 13001 MW; 4F83B229C468B15F CRC64; MFDPLSLKYD AAGLIPAIAQ DAASGEVLMM AWMNADAVAR TLSTGRVTYW SRSRASFWIK GESSGHVQQL VEMRVDCDRD CLLVLVEQTG PACHTNRRSC FYTGIRDGAE VVLSEPMV //