HIS3_MYCTA
ID HIS3_MYCTA Reviewed; 115 AA.
AC A5U2W2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=MRA_1616;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ73362.1; -; Genomic_DNA.
DR RefSeq; WP_003407963.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U2W2; -.
DR SMR; A5U2W2; -.
DR STRING; 419947.MRA_1616; -.
DR EnsemblBacteria; ABQ73362; ABQ73362; MRA_1616.
DR GeneID; 45425574; -.
DR KEGG; mra:MRA_1616; -.
DR eggNOG; COG0139; Bacteria.
DR HOGENOM; CLU_048577_5_1_11; -.
DR OMA; TGYRSCF; -.
DR OrthoDB; 1842189at2; -.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000001988; 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..115
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /id="PRO_1000063418"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 81
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 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 97
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 104
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 115 AA; 12465 MW; 07519F1E5D4D6D83 CRC64;
MTLDPKIAAR LKRNADGLVT AVVQERGSGD VLMVAWMNDE ALARTLQTRE ATYYSRSRAE
QWVKGATSGH TQHVHSVRLD CDGDAVLLTV DQVGGACHTG DHSCFDAAVL LEPDD
