HIS3_VESOH
ID HIS3_VESOH Reviewed; 126 AA.
AC A5CXC7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=COSY_0275;
OS Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Vesicomyosocius.
OX NCBI_TaxID=412965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA;
RX PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T.,
RA Kato C., Kitagawa M., Kato I., Maruyama T.;
RT "Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea
RT clam, Calyptogena okutanii.";
RL Curr. Biol. 17:881-886(2007).
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; AP009247; BAF61404.1; -; Genomic_DNA.
DR RefSeq; WP_011929674.1; NC_009465.1.
DR AlphaFoldDB; A5CXC7; -.
DR SMR; A5CXC7; -.
DR STRING; 412965.COSY_0275; -.
DR EnsemblBacteria; BAF61404; BAF61404; COSY_0275.
DR KEGG; vok:COSY_0275; -.
DR eggNOG; COG0139; Bacteria.
DR HOGENOM; CLU_048577_5_0_6; -.
DR OMA; TGYRSCF; -.
DR OrthoDB; 1842189at2; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000000247; 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; -; 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; Cytoplasm; Histidine biosynthesis; Hydrolase;
KW Magnesium; Metal-binding; Zinc.
FT CHAIN 1..126
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /id="PRO_0000319723"
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; 14728 MW; A8680C82D5ABECEC CRC64;
MSALKQIKFD EKGLIPAISQ DFKTGEILMF AWMNQESLKL TIKKQQAVYY SRSRQKIWFK
GEESGHIQHI KEIFTDCDND VILLKIEQIG GISCHTGRIS CFFQQLDKKN WKIITNMIKN
PRDIYG