ID GLO2_BRUSI Reviewed; 260 AA. AC B0CIU0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 02-SEP-2026, entry version 85. 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}; GN OrderedLocusNames=BSUIS_A1776; OS Brucella suis (strain ATCC 23445 / NCTC 10510). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella; OC Brucella melitensis group. OX NCBI_TaxID=470137; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23445 / NCTC 10510; RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., RA Bruce D., Detter C., Munk C., Brettin T.S.; RT "Brucella suis ATCC 23445 whole genome shotgun sequencing project."; RL Submitted (DEC-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; Evidence={ECO:0000255|HAMAP- CC 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; CP000911; ABY38793.1; -; Genomic_DNA. DR RefSeq; WP_002965004.1; NC_010169.1. DR AlphaFoldDB; B0CIU0; -. DR SMR; B0CIU0; -. DR GeneID; 93017735; -. DR GeneID; 99645033; -. DR KEGG; bmt:BSUIS_A1776; -. DR HOGENOM; CLU_030571_4_1_5; -. DR UniPathway; UPA00619; UER00676. DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051596; P:methylglyoxal catabolic process; IEA:InterPro. DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1. DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1. DR HAMAP; MF_01374; Glyoxalase_2; 1. DR InterPro; IPR035680; Clx_II_MBL. DR InterPro; IPR050110; Glyoxalase_II_hydrolase. DR InterPro; IPR032282; HAGH_C. DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro. DR NCBIfam; TIGR03413; GSH_gloB; 1. DR PANTHER; PTHR43705; HYDROXYACYLGLUTATHIONE HYDROLASE; 1. DR PANTHER; PTHR43705:SF1; HYDROXYACYLGLUTATHIONE HYDROLASE GLOB; 1. 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; Metallo-hydrolase/oxidoreductase; 1. PE 3: Inferred from homology; KW Hydrolase; Metal-binding; Zinc. FT CHAIN 1..260 FT /note="Hydroxyacylglutathione hydrolase" FT /id="PRO_1000087278" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 138 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 138 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 176 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" SQ SEQUENCE 260 AA; 29140 MW; 56A7D32D568319BA CRC64; MHRMEQRLEI EQFICRSDNY GVLIHDPESA LTATIDAPDA YAIEAALERR GWTLDFIFTT HHHLDHVEGN EPLKEKFGVS IIGPEAEKAK IPGIDRTVKG GDEFTFGLFK VKVISTPGHT AGGISYYLPD AKVVFTGDTL FALGCGRLFE GTPATMFHSL EKLVALPGDT ALYCGHEYTQ NNARFALTID PDNSALKERA KEIARLRAHE RMTLPSTIAL EMATNPFLRW HDRTIRARLG LQDAPDEAVF AEIRKRKDMF //