ID A2QD33_ASPNC Unreviewed; 204 AA.
AC A2QD33;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Contig An02c0160, genomic contig {ECO:0000313|EMBL:CAK47695.1};
DE EC=4.4.1.5 {ECO:0000313|EMBL:CAK47695.1};
GN ORFNames=An02g05670 {ECO:0000313|EMBL:CAK47695.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK47695.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK47695.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270011; CAK47695.1; -; Genomic_DNA.
DR RefSeq; XP_001399703.2; XM_001399666.2.
DR AlphaFoldDB; A2QD33; -.
DR EnsemblFungi; CAK47695; CAK47695; An02g05670.
DR GeneID; 4979056; -.
DR VEuPathDB; FungiDB:An02g05670; -.
DR HOGENOM; CLU_046006_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR PANTHER; PTHR10374; LACTOYLGLUTATHIONE LYASE GLYOXALASE I; 1.
DR PANTHER; PTHR10374:SF19; LYASE (GLO1), PUTATIVE (AFU_ORTHOLOGUE AFUA_2G13550)-RELATED; 1.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR PROSITE; PS51819; VOC; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:CAK47695.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 34..204
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 22728 MW; 20AEED446D7454FB CRC64;
MPSASPSSPF EAGIYLPGGH NTDPPMTSDT DGYRLNHFML RIRDPQRTLH FYIDLMGMRT
IFTMNAGPFT MYYLGYPPTP SDRADLSAWA SRVANVRELT QTIGLLEFYH THGTEKDDEF
RVSSGNSPPN LGFGHLGFTV PDVPAAVERL RREGVHVLKD LGDSSRESVP LSTWEEHRGF
GTGDLHPKFK EIYDQIACVA DPVG
//
