HIS3_METVA
ID HIS3_METVA Reviewed; 136 AA.
AC Q50837;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 88.
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, ECO:0000269|PubMed:9931020};
GN Name=hisI {ECO:0000255|HAMAP-Rule:MF_01021};
OS Methanococcus vannielii.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=2187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3018439; DOI=10.1007/bf00330200;
RA Beckler G.S., Reeve J.N.;
RT "Conservation of primary structure in the hisI gene of the archaebacterium,
RT Methanococcus vannielii, the eubacterium Escherichia coli, and the
RT eucaryote Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 204:133-140(1986).
RN [2]
RP PROTEIN SEQUENCE OF 2-26, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=9931020; DOI=10.1021/bi982475x;
RA D'Ordine R.L., Klem T.J., Davisson V.J.;
RT "N1-(5'-phosphoribosyl)adenosine-5'-monophosphate cyclohydrolase:
RT purification and characterization of a unique metalloenzyme.";
RL Biochemistry 38:1537-1546(1999).
CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of
CC phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021,
CC ECO:0000269|PubMed:9931020}.
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, ECO:0000269|PubMed:9931020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01021,
CC ECO:0000269|PubMed:9931020};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01021,
CC ECO:0000269|PubMed:9931020};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01021,
CC ECO:0000269|PubMed:9931020};
CC Note=Binds 1 zinc ion per subunit. May play a cocatalytic role and/or a
CC structural role. {ECO:0000255|HAMAP-Rule:MF_01021,
CC ECO:0000269|PubMed:9931020};
CC -!- ACTIVITY REGULATION: Reversibly inhibited by EDTA and free zinc ions.
CC Enzyme is inactivated by dialysis against 1,10-phenanthroline, which is
CC a zinc specific chelator. {ECO:0000269|PubMed:9931020}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.9 uM for phosphoribosyl-AMP {ECO:0000269|PubMed:9931020};
CC Note=kcat is 4.1 sec(-1).;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:9931020};
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, ECO:0000269|PubMed:9931020}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01021,
CC ECO:0000269|PubMed:9931020}.
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; X04021; CAA27649.1; -; Genomic_DNA.
DR PIR; S28723; S28723.
DR AlphaFoldDB; Q50837; -.
DR SMR; Q50837; -.
DR GeneID; 5324753; -.
DR OMA; YSCFHYK; -.
DR BRENDA; 3.5.4.19; 3267.
DR UniPathway; UPA00031; UER00008.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Direct protein sequencing;
KW Histidine biosynthesis; Hydrolase; Magnesium; Metal-binding; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9931020"
FT CHAIN 2..136
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /id="PRO_0000136512"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 93
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 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01021"
FT BINDING 109
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 116
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 136 AA; 15621 MW; 74CA4F7DA48495E0 CRC64;
MGIKDIDIKE NFGKIVQNMD LKFRKIDDKE LLIAIAIDKY KNVLMTAFMD KESLKMTLKT
GLMHYFSTSR NKIWMKGEES KNVQKVLEVF KDCDGDALLF IVEQTGWACH EGYMSCFHNK
VDLNTGNSTV IGDKLD
