ID A0A059CKZ3_EUCGR Unreviewed; 386 AA.
AC A0A059CKZ3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00012081};
DE EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081};
DE AltName: Full=Glyoxalase I {ECO:0000256|ARBA:ARBA00030537};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_C00588 {ECO:0000313|EMBL:KCW79143.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW79143.1};
RN [1] {ECO:0000313|EMBL:KCW79143.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW79143.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione.
CC {ECO:0000256|ARBA:ARBA00003610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal;
CC Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474,
CC ChEBI:CHEBI:57925; EC=4.4.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000817};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR604361-3};
CC Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are
CC bound between subunits. {ECO:0000256|PIRSR:PIRSR604361-3};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005008}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
CC {ECO:0000256|ARBA:ARBA00010363}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK198755; KCW79143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059CKZ3; -.
DR STRING; 71139.A0A059CKZ3; -.
DR EnsemblPlants; KCW79143; KCW79143; EUGRSUZ_C00588.
DR Gramene; KCW79143; KCW79143; EUGRSUZ_C00588.
DR eggNOG; KOG2943; Eukaryota.
DR InParanoid; A0A059CKZ3; -.
DR OMA; VQICSAM; -.
DR UniPathway; UPA00619; UER00675.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR NCBIfam; TIGR00068; glyox_I; 1.
DR PANTHER; PTHR46036; LACTOYLGLUTATHIONE LYASE; 1.
DR PANTHER; PTHR46036:SF18; LACTOYLGLUTATHIONE LYASE; 1.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS51819; VOC; 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604361-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR604361-3}.
FT DOMAIN 125..248
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 254..378
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT ACT_SITE 244
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KCW79143.1"
SQ SEQUENCE 386 AA; 43022 MW; 8A17C1D9014D9596 CRC64;
DFCFRSSVTK QVQICSAMLT MITVLVPSPF SLPRKHSFSS RCSFKLCCSD NRSNESSCSN
FSRRLALFQL GTAIPQSQVL GVKASELLRP AESTTKTNNI GNVAEMNSNL TEDSALRWAK
KDKRRMLHAV YRVGDLDKTI KFYTECFGMK LLRKRDIPEE RYSNAFLGYG PEDSHFTVEL
TYNYGTDKYN VGNGLHFGIT LDDVAKAVNL VKAKGGKVIK ESVLLDGNSK IITYVEDPDG
YKFELSEAAT TPEPLHHVKL CVGNLDRSIN FYKKAFGMDL LSKQDNPEYK YSEVTLGYGP
EDTNPVLKLT YNYGVTVYDK GDGYAQIAIG TDDVYKTAEA IKLFDGIIAL EPGPLPGINT
KITACLDPDG WKSVFVDNVD FLKELE
//
