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Database: UniProt
Entry: A0A1Q3D1Q3_CEPFO
LinkDB: A0A1Q3D1Q3_CEPFO
Original site: A0A1Q3D1Q3_CEPFO 
ID   A0A1Q3D1Q3_CEPFO        Unreviewed;       319 AA.
AC   A0A1Q3D1Q3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=CFOL_v3_29803 {ECO:0000313|EMBL:GAV86372.1};
OS   Cephalotus follicularis (Albany pitcher plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Oxalidales; Cephalotaceae; Cephalotus.
OX   NCBI_TaxID=3775 {ECO:0000313|EMBL:GAV86372.1, ECO:0000313|Proteomes:UP000187406};
RN   [1] {ECO:0000313|Proteomes:UP000187406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. St1 {ECO:0000313|Proteomes:UP000187406};
RA   Fukushima K., Hasebe M., Fang X.;
RT   "Cephalotus genome sequencing.";
RL   Submitted (APR-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAV86372.1}.
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DR   EMBL; BDDD01003878; GAV86372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3D1Q3; -.
DR   STRING; 3775.A0A1Q3D1Q3; -.
DR   InParanoid; A0A1Q3D1Q3; -.
DR   OrthoDB; 2076575at2759; -.
DR   UniPathway; UPA00619; UER00675.
DR   Proteomes; UP000187406; 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; 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:SF5; LACTOYLGLUTATHIONE LYASE; 1.
DR   Pfam; PF00903; Glyoxalase; 2.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR   PROSITE; PS00934; GLYOXALASE_I_1; 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:UP000187406};
KW   Zinc {ECO:0000256|PIRSR:PIRSR604361-3}.
FT   DOMAIN          57..181
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          187..311
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   ACT_SITE        177
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT   BINDING         111
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         129
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         177
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:GAV86372.1"
FT   NON_TER         319
FT                   /evidence="ECO:0000313|EMBL:GAV86372.1"
SQ   SEQUENCE   319 AA;  35573 MW;  845D810910F0127E CRC64;
     YCYSGVPQSQ FFGLKASKIL RGEDSSIGVS AAGNAAQASI AATQENLLEW VKNDKRRMLH
     VVYRVGDLDR TIKFYTECLG MKLLRKRDIP EERYTNAFLG YGPEDSHFVI ELTYNYGVDK
     YDVGSGFGHF GIAVDDVAKI VELIKAKGGK VTREPGPVKG GSTVIAFVED PDGYKFELLE
     RGPTPEPLCQ VMLRVGDLDR AVNFYEKAFG MELLRKRDNP EYKYTIAMMG YGPEDKNVVL
     ELTYNYGVTE YDKGNAYAQI AIGTDDVYRT AEAIKLYGGK VTREPGPLPG INTKITACLD
     PDGWKTVFVD NIDFLKELE
//
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