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GLO2_MARMS
ID   GLO2_MARMS              Reviewed;         257 AA.
AC   A6VVZ9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Mmwyl1_1702;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) 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}.
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DR   EMBL; CP000749; ABR70628.1; -; Genomic_DNA.
DR   RefSeq; WP_012069411.1; NC_009654.1.
DR   AlphaFoldDB; A6VVZ9; -.
DR   SMR; A6VVZ9; -.
DR   STRING; 400668.Mmwyl1_1702; -.
DR   EnsemblBacteria; ABR70628; ABR70628; Mmwyl1_1702.
DR   KEGG; mmw:Mmwyl1_1702; -.
DR   eggNOG; COG0491; Bacteria.
DR   HOGENOM; CLU_030571_4_1_6; -.
DR   OMA; NYIWLLQ; -.
DR   OrthoDB; 733552at2; -.
DR   UniPathway; UPA00619; UER00676.
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   PIRSF; PIRSF005457; Glx; 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; Zinc.
FT   CHAIN           1..257
FT                   /note="Hydroxyacylglutathione hydrolase"
FT                   /id="PRO_1000087283"
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="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01374"
SQ   SEQUENCE   257 AA;  28763 MW;  27CB2D185589451B CRC64;
     MTIFPLPAFN DNYIWIIQDK DSSGIWAVDP GKADVVLNFC HEYQKTLTGI LITHHHKDHT
     GGVAELKQHS NCPVYGPEHL TELVTHPVDD GDRILVFSKV FTVIATPGHT LDHLCYFSEQ
     ETPILLSGDT LFKGGCGRIM EGTHEQMLAA MIKISGLPND TLIYGTHEYT LANYRFALSL
     EPNNKDLIES NITCQKLRTE EKPTLPTKLS IEKKTNPFLR SHIEALKIQA AQQLNEIPAE
     NPIGAFSQVR RAKDSFS
 
 
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