GLO2_NEIG1
ID GLO2_NEIG1 Reviewed; 250 AA.
AC Q5F7J0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Hydroxyacylglutathione hydrolase {ECO:0000255|HAMAP-Rule:MF_01374};
DE EC=3.1.2.6 {ECO:0000255|HAMAP-Rule:MF_01374};
DE AltName: Full=Glyoxalase II {ECO:0000255|HAMAP-Rule:MF_01374};
DE Short=Glx II {ECO:0000255|HAMAP-Rule:MF_01374};
GN Name=gloB {ECO:0000255|HAMAP-Rule:MF_01374}; OrderedLocusNames=NGO1187;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid. {ECO:0000255|HAMAP-
CC Rule:MF_01374}.
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:0000255|HAMAP-Rule:MF_01374};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01374};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01374};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_01374}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01374}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000255|HAMAP-Rule:MF_01374}.
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; AE004969; AAW89847.1; -; Genomic_DNA.
DR RefSeq; WP_003689617.1; NC_002946.2.
DR RefSeq; YP_208259.1; NC_002946.2.
DR AlphaFoldDB; Q5F7J0; -.
DR SMR; Q5F7J0; -.
DR STRING; 242231.NGO_1187; -.
DR EnsemblBacteria; AAW89847; AAW89847; NGO_1187.
DR GeneID; 66753907; -.
DR KEGG; ngo:NGO_1187; -.
DR PATRIC; fig|242231.10.peg.1394; -.
DR HOGENOM; CLU_030571_4_1_4; -.
DR OMA; NYIWLLQ; -.
DR UniPathway; UPA00619; UER00676.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..250
FT /note="Hydroxyacylglutathione hydrolase"
FT /id="PRO_0000309662"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
SQ SEQUENCE 250 AA; 27810 MW; A7841E49F2F600F5 CRC64;
MKITPVKALT DNYIWMIQHG NHAVCVDPSE PSPVLEFLVR NRLMLAQTWV THPHPDHEGG
AAALWRGYME SPVYGESDIE AATHTVTAGT RFTFGNGQVT VWATPGHTDR HTSYLLETSD
GIHVFCGDTL FSAGCGRVFT GTVEQLYDNF QRFNQLPEGT LFYPAHEYTA ANLRFAAHIE
PDNADIQTAL KAAEHTPTLP VTLAHERRVN PFLRTEIPAV RQRAEALVGK TLNSGLEVFA
ALRELKNAYR
