GLO2_DANRE
ID GLO2_DANRE Reviewed; 303 AA.
AC Q6P963;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 101.
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; ORFNames=zgc:73161;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) 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 -!- 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=Q6P963-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P963-2; Sequence=VSP_037934;
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met-
CC 44 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60913.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH66607.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAQ97789.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY398356; AAQ97789.1; ALT_INIT; mRNA.
DR EMBL; BC060913; AAH60913.1; ALT_INIT; mRNA.
DR EMBL; BC066607; AAH66607.1; ALT_INIT; mRNA.
DR RefSeq; NP_956337.1; NM_200043.2. [Q6P963-2]
DR RefSeq; XP_005163922.1; XM_005163865.3. [Q6P963-1]
DR RefSeq; XP_009297606.1; XM_009299331.2. [Q6P963-1]
DR AlphaFoldDB; Q6P963; -.
DR SMR; Q6P963; -.
DR STRING; 7955.ENSDARP00000034038; -.
DR PaxDb; Q6P963; -.
DR Ensembl; ENSDART00000034373; ENSDARP00000034038; ENSDARG00000025338. [Q6P963-1]
DR Ensembl; ENSDART00000134208; ENSDARP00000122766; ENSDARG00000025338. [Q6P963-1]
DR GeneID; 336977; -.
DR KEGG; dre:336977; -.
DR CTD; 3029; -.
DR ZFIN; ZDB-GENE-030131-8921; hagh.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00940000159176; -.
DR HOGENOM; CLU_030571_4_0_1; -.
DR InParanoid; Q6P963; -.
DR OMA; NYIWLLQ; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; Q6P963; -.
DR TreeFam; TF105273; -.
DR Reactome; R-DRE-70268; Pyruvate metabolism.
DR PRO; PR:Q6P963; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000025338; Expressed in liver and 23 other tissues.
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 Alternative initiation; Cytoplasm; Hydrolase; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..303
FT /note="Hydroxyacylglutathione hydrolase, mitochondrial"
FT /id="PRO_0000382743"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT BINDING 292..295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16775"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15520368, ECO:0000303|Ref.2"
FT /id="VSP_037934"
SQ SEQUENCE 303 AA; 33806 MW; 0578D00267A11F85 CRC64;
MWFRSLAVSA CTVGVLGALS QKFAPTALFH SAIRKSSLVE QSDMKVELLP ALTDNYMYLL
IDEETKEAAI VDPVEPQKVV DAVKKHGVKL KTVLTTHHHW DHAGGNEKLV KLMPGLTVYG
GDDRVGALTQ KVTHYNTFKV GSLNVKCLFT PCHTSGHICY FVTKENSTEA PAVFTGDTLF
VAGCGKFFEG TADEMYKALI EVLGRLPPET RVYCGHEYTI NNLKFARHVE PNNEVIRTKL
AWAKEKYDNG EPTIPSTVAE EFTFNPFMRV REKSVLEHAG TSDPIEAMRS IRKEKDGFRV
PKN
