ID A6UCK2_SINMW Unreviewed; 256 AA. AC A6UCK2; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 02-SEP-2026, entry version 99. DE RecName: Full=Hydroxyacylglutathione hydrolase {ECO:0000256|HAMAP-Rule:MF_01374}; DE EC=3.1.2.6 {ECO:0000256|HAMAP-Rule:MF_01374}; DE AltName: Full=Glyoxalase II {ECO:0000256|HAMAP-Rule:MF_01374}; DE Short=Glx II {ECO:0000256|HAMAP-Rule:MF_01374}; GN Name=gloB {ECO:0000256|HAMAP-Rule:MF_01374}; GN OrderedLocusNames=Smed_2552 {ECO:0000313|EMBL:ABR61382.1}; OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR61382.1, ECO:0000313|Proteomes:UP000001108}; RN [1] {ECO:0000313|EMBL:ABR61382.1, ECO:0000313|Proteomes:UP000001108} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM419 {ECO:0000313|EMBL:ABR61382.1, RC ECO:0000313|Proteomes:UP000001108}; RX PubMed=21304680; DOI=10.4056/sigs.43526; RA Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R., RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M., RA Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V., RA Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.; RT "Complete genome sequence of the Medicago microsymbiont Ensifer RT (Sinorhizobium) medicae strain WSM419."; RL Stand. Genomic Sci. 2:77-86(2010). CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- CC glutathione to form glutathione and D-lactic acid. {ECO:0000256|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:0000256|ARBA:ARBA00001623, ECO:0000256|HAMAP- CC Rule:MF_01374}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01374}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01374}; CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation; CC (R)-lactate from methylglyoxal: step 2/2. CC {ECO:0000256|ARBA:ARBA00004963, ECO:0000256|HAMAP-Rule:MF_01374}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01374}. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC Glyoxalase II family. {ECO:0000256|ARBA:ARBA00006759, CC ECO:0000256|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; CP000738; ABR61382.1; -; Genomic_DNA. DR RefSeq; WP_012066773.1; NC_009636.1. DR AlphaFoldDB; A6UCK2; -. DR STRING; 366394.Smed_2552; -. DR GeneID; 61611920; -. DR KEGG; smd:Smed_2552; -. DR PATRIC; fig|366394.8.peg.5744; -. DR eggNOG; COG0491; Bacteria. DR HOGENOM; CLU_030571_4_1_5; -. DR OrthoDB; 9802248at2; -. DR UniPathway; UPA00619; UER00676. DR Proteomes; UP000001108; Chromosome. DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051596; P:methylglyoxal catabolic process; IEA:UniProtKB-UniRule. 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01374}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01374}; Reference proteome {ECO:0000313|Proteomes:UP000001108}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01374}. FT DOMAIN 14..172 FT /note="Metallo-beta-lactamase" FT /evidence="ECO:0000259|SMART:SM00849" FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374" FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374" FT BINDING 115 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374" FT BINDING 172 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374" SQ SEQUENCE 256 AA; 28312 MW; C3E2A72E0FFAD148 CRC64; MAALELDLFL CRTDNYGVLL HDRLSGATAS IDAPEERPIL DALERRSWQL THILTTHHHG DHVAGNIGLK ERFGVTIIGP KNESPKIPGI DRSVGHGDRF DFAGHPVEVI ETPGHTAGHV CYHFPEDKLL FAADTLFALG CGRLFEGTPE TMWQSLSRLM ALPDDTAIYF GHEYTLANAR FAVTVDPENT ALKERAAEIE ETRSDGGFTA PTTMGLEKRT NPFLRADDPK IRAFLGMDKA SDAAVFAEIR KRKDSF //