ID A0A1A9NAJ0_9BURK Unreviewed; 263 AA.
AC A0A1A9NAJ0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ORFNames=A6V37_23790 {ECO:0000313|EMBL:OAJ62070.1};
OS Paraburkholderia ginsengiterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1462993 {ECO:0000313|EMBL:OAJ62070.1, ECO:0000313|Proteomes:UP000078116};
RN [1] {ECO:0000313|EMBL:OAJ62070.1, ECO:0000313|Proteomes:UP000078116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY85 {ECO:0000313|EMBL:OAJ62070.1,
RC ECO:0000313|Proteomes:UP000078116};
RA Dobritsa A.P., Kutumbaka K., Samadpour M.;
RT "Reclassification of Paraburkholderia panaciterrae (Farh et al. 2015)
RT Dobritsa & Samadpour 2016 as a later homotypic synonym of Paraburkholderia
RT ginsengiterrae (Farh et al. 2015) Dobritsa & Samadpour 2016.";
RL Submitted (APR-2016) 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: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;
CC Evidence={ECO:0000256|HAMAP-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAJ62070.1}.
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DR EMBL; LXKA01000187; OAJ62070.1; -; Genomic_DNA.
DR RefSeq; WP_064268413.1; NZ_LXKA01000187.1.
DR AlphaFoldDB; A0A1A9NAJ0; -.
DR STRING; 1462993.A6V36_03395; -.
DR OrthoDB; 9802248at2; -.
DR UniPathway; UPA00619; UER00676.
DR Proteomes; UP000078116; Unassembled WGS sequence.
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; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01374}.
FT DOMAIN 14..174
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
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="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
SQ SEQUENCE 263 AA; 28682 MW; 434097EAA848E2A3 CRC64;
MNALEYVPVP AFDDNYIWVV SDGHHAVVVD PGEAAPVQAY LAKRGWRLSA ILLTHHHQDH
VGGVADLLNG QAVPVYGPAG EAIERLTHRL KNGDHVSIAV PALEFSVLEV PGHTSGHIAY
FQAADPRGVP HVFCGDTLFA CGCGRLFEGT PRQMLASLDS LAALPGATEV HCAHEYTLSN
IRFALACEPG NAELQAWRDR ASDLRARGVP TLPTTVAHER AVNPFLRAGE PAVQASLQDQ
LHEKVSDRLT AFTLMREWKN RFR
//
