GLO2_BOVIN
ID GLO2_BOVIN Reviewed; 308 AA.
AC Q3B7M2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Hydroxyacylglutathione hydrolase, mitochondrial;
DE EC=3.1.2.6 {ECO:0000250|UniProtKB:Q16775};
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
DE Flags: Precursor;
GN Name=HAGH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) 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.
CC {ECO:0000250|UniProtKB:Q16775}.
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:0000250|UniProtKB:Q16775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21865;
CC Evidence={ECO:0000250|UniProtKB:Q16775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione + H2O = (R)-lactate + glutathione +
CC H(+); Xref=Rhea:RHEA:25245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=3.1.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q16775};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25246;
CC Evidence={ECO:0000250|UniProtKB:Q16775};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q16775};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q16775}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q16775}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q16775}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q3B7M2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3B7M2-2; Sequence=VSP_037927;
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 49 of isoform 1. Alternative initiation has been proven in human.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
CC -!- CAUTION: Only one single gene encoding glyoxalase II has been
CC identified in vertebrates. In yeast and higher plants, separate genes
CC encode the cytosolic and mitochondrial forms of glyoxalase II.
CC {ECO:0000305}.
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DR EMBL; BC107545; AAI07546.1; -; mRNA.
DR RefSeq; NP_001030351.1; NM_001035274.1. [Q3B7M2-1]
DR AlphaFoldDB; Q3B7M2; -.
DR SMR; Q3B7M2; -.
DR STRING; 9913.ENSBTAP00000026635; -.
DR BindingDB; Q3B7M2; -.
DR ChEMBL; CHEMBL3627591; -.
DR PaxDb; Q3B7M2; -.
DR PeptideAtlas; Q3B7M2; -.
DR Ensembl; ENSBTAT00000026635; ENSBTAP00000026635; ENSBTAG00000019998. [Q3B7M2-1]
DR GeneID; 509274; -.
DR KEGG; bta:509274; -.
DR CTD; 3029; -.
DR VEuPathDB; HostDB:ENSBTAG00000019998; -.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00940000159176; -.
DR HOGENOM; CLU_030571_4_0_1; -.
DR InParanoid; Q3B7M2; -.
DR OMA; NYIWLLQ; -.
DR TreeFam; TF105273; -.
DR UniPathway; UPA00619; UER00676.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000019998; Expressed in liver and 106 other tissues.
DR ExpressionAtlas; Q3B7M2; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; -; 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 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; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative initiation; Cytoplasm; Hydrolase; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..308
FT /note="Hydroxyacylglutathione hydrolase, mitochondrial"
FT /id="PRO_0000309592"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 191..193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 221..223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 297..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KB8"
FT MOD_RES 229
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT MOD_RES 229
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KB8"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037927"
SQ SEQUENCE 308 AA; 34089 MW; B67A0140178AF9C5 CRC64;
MVLGRGLLGR WSVAELGAVC ARLGLGPALL GSLHHLGLRK SLTVDQGTMK VELLPALTDN
YMYLLIDEDT KEAAIVDPVQ PQKVVETARK HGVKLTTVLT THHHWDHAGG NEKLVKLEPG
LKVYGGDDRI GALTHKVTHL STLQVGSLHV KCLSTPCHTS GHICYFVTKP NSPEPPAVFT
GDTLFVAGCG KFYEGTADEM YKALLEVLGR LPADTRVYCG HEYTINNLKF ARHVEPDNTA
VREKLAWAKE KYSIGEPTVP STIAEEFTYN PFMRVREKTV QQHAGETEPV ATMRAIRKEK
DQFKMPRD
