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Database: UniProt
Entry: A0A094BDN2_9PEZI
LinkDB: A0A094BDN2_9PEZI
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ID   A0A094BDN2_9PEZI        Unreviewed;       342 AA.
AC   A0A094BDN2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=V494_03802 {ECO:0000313|EMBL:KFY39846.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY39846.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY39846.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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}.
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:KFY39846.1}.
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DR   EMBL; JPJW01001253; KFY39846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094BDN2; -.
DR   STRING; 1420907.A0A094BDN2; -.
DR   HOGENOM; CLU_046006_0_1_1; -.
DR   OrthoDB; 245930at2759; -.
DR   UniPathway; UPA00619; UER00675.
DR   Proteomes; UP000029288; 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; 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:UP000029288};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR604361-3}.
FT   DOMAIN          39..180
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   DOMAIN          198..333
FT                   /note="VOC"
FT                   /evidence="ECO:0000259|PROSITE:PS51819"
FT   ACT_SITE        176
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604361-1"
FT   BINDING         102
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         176
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   342 AA;  39241 MW;  5F172B26ED0C15CF CRC64;
     MSLFRTLQRT FRFSTPRFGV VSSDSRSLAT MASKTESYKF NHTMLRVKDP KESSKFYEFL
     GMKLINKIEQ PESKFDLYFF GYDNPKASSH GKVWSDREGL VELTHNYGTE NDPNYKVNNG
     NEEPHRGFGH LCISVDNLQA ACQRLEDAGY TFQKKLSEGR MKYIAFVRDP DGYWIEIIGQ
     KSLEETEGVT TTDVETYVMN HSMIRVKSSS SSLLFYQEVL GMSLLRTHEM PEAKFNVYFL
     GYPNSATGAH REGLLELTWN YGTEADESFS YHNGNAEPQG FGHICVSVDD LDAACARFDE
     VGAKWKKRLT EGRMKNVAFL LDPDGYWVEV IQNEKLKERA KW
//
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