ID A0A3B6NRC2_WHEAT Unreviewed; 325 AA.
AC A0A3B6NRC2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
GN ORFNames=CFC21_083583 {ECO:0000313|EMBL:KAF7079338.1}, CFC21_083586
GN {ECO:0000313|EMBL:KAF7079341.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6A02G215400.1};
RN [1] {ECO:0000313|EMBL:KAF7079338.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7079338.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6A02G215400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6A02G215400.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS6A02G215400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7079338.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7079338.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CM022226; KAF7079338.1; -; Genomic_DNA.
DR EMBL; CM022226; KAF7079341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6NRC2; -.
DR SMR; A0A3B6NRC2; -.
DR STRING; 4565.A0A3B6NRC2; -.
DR PaxDb; 4565-Traes_6AL_2063C3615-4; -.
DR EnsemblPlants; TraesCS6A02G215400.1; TraesCS6A02G215400.1; TraesCS6A02G215400.
DR Gramene; TraesCAD_scaffold_041792_01G000200.1; TraesCAD_scaffold_041792_01G000200.1; TraesCAD_scaffold_041792_01G000200.
DR Gramene; TraesCLE_scaffold_016489_01G000500.1; TraesCLE_scaffold_016489_01G000500.1; TraesCLE_scaffold_016489_01G000500.
DR Gramene; TraesCS6A02G215400.1; TraesCS6A02G215400.1; TraesCS6A02G215400.
DR Gramene; TraesCS6A03G0592300.1; TraesCS6A03G0592300.1.CDS; TraesCS6A03G0592300.
DR Gramene; TraesKAR6A01G0243750.4; cds.TraesKAR6A01G0243750.4; TraesKAR6A01G0243750.
DR Gramene; TraesPAR_scaffold_061450_01G000200.1; TraesPAR_scaffold_061450_01G000200.1; TraesPAR_scaffold_061450_01G000200.
DR OMA; YWVEVIG; -.
DR OrthoDB; 2076575at2759; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000019116; Chromosome 6A.
DR Proteomes; UP000815260; Chromosome 6A.
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 CDD; cd16358; GlxI_Ni; 1.
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:SF2; LACTOYLGLUTATHIONE LYASE GLX1; 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 Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Zinc {ECO:0000256|PIRSR:PIRSR604361-3}.
FT DOMAIN 58..183
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 189..317
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT BINDING 112
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 130
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 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"
SQ SEQUENCE 325 AA; 36301 MW; 492412177D5A9D9A CRC64;
MKGVLQKPLE PPQRGSKRNQ TESSRLSAGS NFRGMATGSE AGKPAEVVLE WPKQDKKRML
HAVYRVGDLD RTIKCYTECF GMKLLRKRDV PEEKYTNAFL GFGPEDTNFA LELTYNYGVD
KYDIGAGFGH FAIANEDVYK LAETIKSSSC CKITREPGPV KGGSTVIAFA QDPDGYMFEL
IQRGPTPEPL CQVMLRVGDL DRSIMFYEKA LGMKLLRKKD VPQYKYTIAM MGYAEEDKTT
VLELTYNYGV TEYNKGNAYA QVAIGTDDVY KSAEAVELVT KELGGKILRQ PGPLPGLNTK
ITSFLDPDGW KVVLVDHADF LKELH
//
