ID A0A093QKF8_9PASS Unreviewed; 286 AA.
AC A0A093QKF8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Hydroxyacylglutathione hydrolase, mitochondrial {ECO:0000256|ARBA:ARBA00039338};
DE EC=3.1.2.6 {ECO:0000256|ARBA:ARBA00011917};
DE AltName: Full=Glyoxalase II {ECO:0000256|ARBA:ARBA00031044};
DE Flags: Fragment;
GN ORFNames=N305_14927 {ECO:0000313|EMBL:KFW84507.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW84507.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW84507.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW84507.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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:0000256|ARBA:ARBA00004015}.
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:0000256|ARBA:ARBA00036971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25246;
CC Evidence={ECO:0000256|ARBA:ARBA00036971};
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:ARBA00036001};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21865;
CC Evidence={ECO:0000256|ARBA:ARBA00036001};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000256|ARBA:ARBA00006759}.
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DR EMBL; KL672051; KFW84507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093QKF8; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro.
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; PTHR11935; BETA LACTAMASE DOMAIN; 1.
DR PANTHER; PTHR11935:SF80; HYDROXYACYLGLUTATHIONE HYDROLASE, MITOCHONDRIAL; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 37..199
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW84507.1"
FT NON_TER 286
FT /evidence="ECO:0000313|EMBL:KFW84507.1"
SQ SEQUENCE 286 AA; 32105 MW; 0F0BF8DECB794998 CRC64;
GPAQLRAFFL HTEHERREPK TVPQADMKVE ILPALTDNYM YLLIDEETKE AAIVDPVNPQ
KVLDAVKKHG VRLTTVLTTH HHWDHAGGNE KLVKMESGLH VYGGDNRVGA LTQKVSHLTA
LQVGSLNVKC LSTPCHTSGH ICYYVTKPNS SEPPAVFTGD TLFVAGCGKF FEGTPEEMYK
ALIEILGSLD PRTRVYCGHE YTINNLKFAR HVEPNNANIQ EKLAWAKARY DSGEPTIPST
IAEEFTYNPF MRVREKTVQQ HAGETDPVRT MGAIRKEKDN FRVPRD
//
