ID GLO2_MARMM Reviewed; 256 AA. AC Q0AM20; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 02-SEP-2026, entry version 96. 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=Mmar10_2381; OS Maricaulis maris (strain MCS10) (Caulobacter maris). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Maricaulales; Maricaulaceae; Maricaulis. OX NCBI_TaxID=394221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., RA Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-2006) 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; CP000449; ABI66673.1; -; Genomic_DNA. DR RefSeq; WP_011644318.1; NC_008347.1. DR AlphaFoldDB; Q0AM20; -. DR SMR; Q0AM20; -. DR STRING; 394221.Mmar10_2381; -. DR KEGG; mmr:Mmar10_2381; -. DR eggNOG; COG0491; Bacteria. DR HOGENOM; CLU_030571_4_1_5; -. DR OrthoDB; 9802248at2; -. DR UniPathway; UPA00619; UER00676. DR Proteomes; UP000001964; Chromosome. 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; Reference proteome; Zinc. FT CHAIN 1..256 FT /note="Hydroxyacylglutathione hydrolase" FT /id="PRO_0000309659" FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 115 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" FT BINDING 172 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01374" SQ SEQUENCE 256 AA; 28458 MW; 25EC9D2CB90AFE46 CRC64; MSELLIRQFP CLSDNYGFLI HDPDSGETAT IDTPDADVIL NEADQAGWSI TQIWNTHHHF DHAGGNETIQ ALTGAKVVAP RYDRHRIPGI SMEVEDGDVI SLGDHKAKVF YTPGHTMGHV CYHMPMDGIA FVGDTLFALG CGRLFEGTPA EMWHSLSRLA ALPDETRIYC AHEYTEANAR FALSIDPDNH DLQVYAAMVE GERARGEPTV PTTIAAEKAA NPFLRPDDPA IRARLGMEHD DDEEVFAEIR RRKDSF //