ID HIS3_MAGMM Reviewed; 129 AA. AC A0LCF4; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 24-JAN-2024, entry version 85. 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}; OrderedLocusNames=Mmc1_3157; OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1; RX PubMed=19465526; DOI=10.1128/aem.02874-08; RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D., RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.; RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic RT coccus strain MC-1."; RL Appl. Environ. Microbiol. 75:4835-4852(2009). 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; CC Evidence={ECO:0000255|HAMAP-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; CC Evidence={ECO:0000255|HAMAP-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; CP000471; ABK45647.1; -; Genomic_DNA. DR RefSeq; WP_011714710.1; NC_008576.1. DR AlphaFoldDB; A0LCF4; -. DR SMR; A0LCF4; -. DR STRING; 156889.Mmc1_3157; -. DR KEGG; mgm:Mmc1_3157; -. DR eggNOG; COG0139; Bacteria. DR HOGENOM; CLU_048577_5_2_5; -. DR OMA; TGYRSCF; -. DR OrthoDB; 9795769at2; -. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000002586; 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; 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..129 FT /note="Phosphoribosyl-AMP cyclohydrolase" FT /id="PRO_0000319695" FT BINDING 79 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 80 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 81 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 83 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021" FT BINDING 96 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 103 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 129 AA; 14620 MW; CBF9C967E72C32AD CRC64; MEKLPDLATL KYNEQGLIPA IAQQYDTGEV LMMAWMNQTS LAETLSTGVA CYWSRSRNRF WRKGESSGQV QTVKAVRLDC DKDTLLLLVD QQGVACHTGR HNCFYLEAQD GSWKTITDPE IDPEELYGK //