HIS3_BRUSI
ID HIS3_BRUSI Reviewed; 139 AA.
AC B0CGM5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=BSUIS_A1120;
OS Brucella suis (strain ATCC 23445 / NCTC 10510).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=470137;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23445 / NCTC 10510;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000911; ABY38176.1; -; Genomic_DNA.
DR RefSeq; WP_004690855.1; NC_010169.1.
DR AlphaFoldDB; B0CGM5; -.
DR SMR; B0CGM5; -.
DR EnsemblBacteria; ABY38176; ABY38176; BSUIS_A1120.
DR GeneID; 45052122; -.
DR GeneID; 55590764; -.
DR KEGG; bmt:BSUIS_A1120; -.
DR HOGENOM; CLU_048577_5_0_5; -.
DR OMA; TGYRSCF; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000008545; Chromosome I.
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..139
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /id="PRO_1000084175"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 92
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 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 110
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 117
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 139 AA; 15308 MW; A150156774661556 CRC64;
MSIFPAQPSD KKAVEEGAAF MPRFDASGLI TAIVTDARDG ELLMVAHMNE EALRLTLETG
IAHYWSRSRK TLWKKGETSG NLQSVVELRT DCDQDALWLK VHVAGDGPTC HTGRRSCFYR
QVVSSGGKVA LTMVSDHDQ
