ID HIS3_DESVH Reviewed; 126 AA. AC P62386; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 104. 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=DVU_0113; OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM OS B-1760 / Hildenborough). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Nitratidesulfovibrio. OX NCBI_TaxID=882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough; RX PubMed=15077118; DOI=10.1038/nbt959; RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., RA Wall J.D., Voordouw G., Fraser C.M.; RT "The genome sequence of the anaerobic, sulfate-reducing bacterium RT Desulfovibrio vulgaris Hildenborough."; RL Nat. Biotechnol. 22:554-559(2004). CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of CC phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta- CC 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:0000255|HAMAP- CC Rule:MF_01021}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01021}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01021}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01021}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01021}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC 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; AE017285; AAS94597.1; -; Genomic_DNA. DR RefSeq; WP_010937424.1; NZ_CABHLV010000001.1. DR RefSeq; YP_009338.1; NC_002937.3. DR AlphaFoldDB; P62386; -. DR SMR; P62386; -. DR STRING; 882.DVU_0113; -. DR PaxDb; 882-DVU_0113; -. DR EnsemblBacteria; AAS94597; AAS94597; DVU_0113. DR KEGG; dvu:DVU_0113; -. DR PATRIC; fig|882.5.peg.111; -. DR eggNOG; COG0139; Bacteria. DR HOGENOM; CLU_048577_5_0_7; -. DR OrthoDB; 9795769at2; -. DR PhylomeDB; P62386; -. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000002194; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 4.10.80.70; -; 1. DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 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 PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1. DR PANTHER; PTHR42945:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 1. DR Pfam; PF01502; PRA-CH; 1. DR SUPFAM; SSF141734; HisI-like; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Hydrolase; KW Magnesium; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..126 FT /note="Phosphoribosyl-AMP cyclohydrolase" FT /id="PRO_0000136476" FT BINDING 76 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 77 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 78 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 80 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 94 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" SQ SEQUENCE 126 AA; 13991 MW; AD4F63840DC10E29 CRC64; MTAFVPDFGK AGGLVPAIAQ DADTGEVLMM AWMNAEAFEM TLKTGEAHYF SRSRGRLWHK GGTSGHTQHI RAVRLDCDSD TILLLVEQRG GAACHEGYRS CFYREMKDGE VSICSPKVFD PKEVYK //