ID A2QL53_ASPNC Unreviewed; 332 AA.
AC A2QL53;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Contig An05c0060, genomic contig {ECO:0000313|EMBL:CAK44919.1};
DE EC=1.13.11.- {ECO:0000313|EMBL:CAK44919.1};
GN ORFNames=An05g02580 {ECO:0000313|EMBL:CAK44919.1};
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:CAK44919.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK44919.1, 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; AM270106; CAK44919.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QL53; -.
DR EnsemblFungi; CAK44919; CAK44919; An05g02580.
DR VEuPathDB; FungiDB:An05g02580; -.
DR HOGENOM; CLU_052361_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 7L.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd07257; THT_oxygenase_C; 1.
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; PTHR43048; METHYLMALONYL-COA EPIMERASE; 1.
DR PANTHER; PTHR43048:SF3; METHYLMALONYL-COA EPIMERASE, MITOCHONDRIAL; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:CAK44919.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 173..299
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 332 AA; 37407 MW; 9C6E3163D156723C CRC64;
MASCHGASIP DITAIGPNQE SIATWRKRCG IQPEKQIRLD LLTALTDFGM YISKQTNDEV
WYRGYGVDQY VYYAKKGDKK FLGGTYEVES YADLERASQL PNGSAIHELI YAPGGGYMVT
IIDPEGFPVN LMYGQQPAKP GEYPENLIFN TETEKPRIRK FQRFVEGPAP VHKLGHYGLC
VKDFSAMVAF YTTTFNLVPT DFLHVGEGND KTNVAVFAHI DRGTDYVDHH TFFMSTNSTS
HVHHCSFEVH DFDTQKLGHQ WLAKRGYTPV WGVGRHILGS QIFDYWWDTT GNMIEHYADG
DIVNEKTPIG YGQAGDSSLA IWGPDVPAWF LK
//
