ID A0A2D3V9W5_9PEZI Unreviewed; 320 AA.
AC A0A2D3V9W5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=lactoylglutathione lyase {ECO:0000256|ARBA:ARBA00012081};
DE EC=4.4.1.5 {ECO:0000256|ARBA:ARBA00012081};
DE AltName: Full=Aldoketomutase {ECO:0000256|ARBA:ARBA00030892};
DE AltName: Full=Ketone-aldehyde mutase {ECO:0000256|ARBA:ARBA00030291};
DE AltName: Full=Methylglyoxalase {ECO:0000256|ARBA:ARBA00032460};
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase {ECO:0000256|ARBA:ARBA00033298};
GN ORFNames=RCC_03045 {ECO:0000313|EMBL:CZT17213.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT17213.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT17213.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT17213.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; FJUY01000003; CZT17213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D3V9W5; -.
DR STRING; 112498.A0A2D3V9W5; -.
DR OrthoDB; 245930at2759; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000225277; Unassembled WGS sequence.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07233; GlxI_Zn; 2.
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; 2.
DR PANTHER; PTHR10374:SF30; LACTOYLGLUTATHIONE LYASE; 1.
DR PANTHER; PTHR10374; LACTOYLGLUTATHIONE LYASE GLYOXALASE I; 1.
DR Pfam; PF00903; Glyoxalase; 2.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR PROSITE; PS00935; GLYOXALASE_I_2; 2.
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:UP000225277};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR604361-3}.
FT DOMAIN 6..147
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT DOMAIN 165..310
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT ACT_SITE 306
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT BINDING 233
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 260
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 306
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 320 AA; 36332 MW; C8B6BE024DB8B3D4 CRC64;
MTDPSSYKFN HTMVKDPKAS VAFYEKLGMS QVNKFEFPDN KFDLYFMAYD SPKSASHGSH
WTDREGIVEL THNYGTESDP NFKVANGNKE PGKGFGHICI SVDNIQAACQ RLEDAGYKFQ
KKLKDGRMHH IAFALDPDEY WVEIIAQNPV NETENVKETD VSTYRMNHSM IRVKDKDVSL
KFYEDIMGMT FLRSSENEAA GFNLYFLGYG GKPKSDDSVN GVNPVASREG ILELTWNYGT
EKEEGKVYHD GNAEPQGFGH ICVSVDDLNA ACQRFEEKGV SWKKRLTDGR MKNVAFVLDP
DGYWIEVIQN EKYKPAPGNY
//
