ID A0A1H2PWT1_9BURK Unreviewed; 280 AA.
AC A0A1H2PWT1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=SAMN05216551_114118 {ECO:0000313|EMBL:SDV51018.1};
OS Chitinasiproducens palmae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Chitinasiproducens.
OX NCBI_TaxID=1770053 {ECO:0000313|EMBL:SDV51018.1, ECO:0000313|Proteomes:UP000243719};
RN [1] {ECO:0000313|Proteomes:UP000243719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS23 {ECO:0000313|Proteomes:UP000243719};
RA Varghese N., Submissions S.;
RL Submitted (SEP-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}.
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DR EMBL; FNLO01000014; SDV51018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2PWT1; -.
DR STRING; 1770053.SAMN05216551_114118; -.
DR UniPathway; UPA00619; UER00676.
DR Proteomes; UP000243719; 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}; Reference proteome {ECO:0000313|Proteomes:UP000243719};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01374}.
FT DOMAIN 29..190
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01374"
SQ SEQUENCE 280 AA; 29782 MW; 3210EF44C7569B94 CRC64;
MYQTSPESTI ATEHRADALV CTALPALQDN YIWVLDDGAQ AVVVDPGQAA PVQAMLRARQ
LQLAAILLTH HHADHVAGVP ALLADAPGAP VFGPAVEAIA TVDRPVRGGE RVAVPGLALD
FQVLDTPGHT RGHIAFYSAD ARLGAPRLFC GDTLFACGCG RLFEGTPEQM HASLGGFAAL
PDTTRVHCAH EYTLANIRFA LACEPGNRVL QAFDREASAL REKGQPTVPT TLGDERARNP
FLRVDVPEIA ATLEARAGRA VPPGAPRFAA LRAWKDVFQP
//
