GLO22_HAEIN
ID GLO22_HAEIN Reviewed; 212 AA.
AC Q57544;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Hydroxyacylglutathione hydrolase GloC {ECO:0000250|UniProtKB:P75849};
DE EC=3.1.2.6 {ECO:0000250|UniProtKB:P75849};
DE AltName: Full=Accessory type II glyoxalase {ECO:0000250|UniProtKB:P75849};
DE AltName: Full=Glyoxalase II 2 {ECO:0000250|UniProtKB:P75849};
DE Short=GlxII-2 {ECO:0000250|UniProtKB:P75849};
GN Name=gloC {ECO:0000250|UniProtKB:P75849}; OrderedLocusNames=HI_1663;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Type II glyoxalase, isozyme of GloB, that hydrolyzes (R)-S-
CC lactoylglutathione to (R)-lactate and glutathione. Plays a role in
CC methylglyoxal (MG) detoxification. {ECO:0000250|UniProtKB:P75849}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy
CC carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
CC Evidence={ECO:0000250|UniProtKB:P75849};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione + H2O = (R)-lactate + glutathione +
CC H(+); Xref=Rhea:RHEA:25245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=3.1.2.6;
CC Evidence={ECO:0000250|UniProtKB:P75849};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q16775};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC {ECO:0000250|UniProtKB:P75849}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
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DR EMBL; L42023; AAC23309.1; -; Genomic_DNA.
DR PIR; D64174; D64174.
DR RefSeq; NP_439805.1; NC_000907.1.
DR RefSeq; WP_005694389.1; NC_000907.1.
DR AlphaFoldDB; Q57544; -.
DR SMR; Q57544; -.
DR STRING; 71421.HI_1663; -.
DR EnsemblBacteria; AAC23309; AAC23309; HI_1663.
DR KEGG; hin:HI_1663; -.
DR PATRIC; fig|71421.8.peg.1741; -.
DR eggNOG; COG0491; Bacteria.
DR HOGENOM; CLU_030571_5_0_6; -.
DR OMA; GAWGTNC; -.
DR PhylomeDB; Q57544; -.
DR BioCyc; HINF71421:G1GJ1-1680-MON; -.
DR UniPathway; UPA00619; UER00676.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 3: Inferred from homology;
KW Detoxification; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..212
FT /note="Hydroxyacylglutathione hydrolase GloC"
FT /id="PRO_0000192358"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
SQ SEQUENCE 212 AA; 23882 MW; 409D4E7DA445F4AA CRC64;
MNIEIIPVTA FQQNCSLIWD DEKNAAIIDP GGEAERLIQR IEELDLNLKV LLLTHGHLDH
VGAAMQLKQH FGVEIWGSNE KDKFLFESLP EQAQRFGLPN IDAFLPDRWF NQEGEILKLD
GFNFEILHLP GHTPGHIGFI EHEKKVAFTG DVLFQGGIGR TDFPRGDYET LISSIRTKLL
PLNDDIIIIA GHGSYTTIGQ EKRSNPFLNS KS
