ID A2QFQ3_ASPNC Unreviewed; 360 AA.
AC A2QFQ3;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Contig An03c0020, genomic contig {ECO:0000313|EMBL:CAK38013.1};
DE EC=1.13.11.- {ECO:0000313|EMBL:CAK38013.1};
GN ORFNames=An03g00350 {ECO:0000313|EMBL:CAK38013.1};
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:CAK38013.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK38013.1, 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; AM270043; CAK38013.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QFQ3; -.
DR EnsemblFungi; CAK38013; CAK38013; An03g00350.
DR VEuPathDB; FungiDB:An03g00350; -.
DR HOGENOM; CLU_052361_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 6R.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd07267; THT_Oxygenase_N; 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; 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:CAK38013.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..360
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002644783"
FT DOMAIN 197..326
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
FT REGION 156..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 41040 MW; B364F97817E21554 CRC64;
MSLWLIDLIA LLPSKWQNWI LPPSTIPVVH NSPQKVQLSR IAHVYFEHAS LEAFTKFAQD
FGFVEAMRKG NTIYYRGYGR DPYVYVASQS PTRRSQFLGA AFVAKDEENF NKAAAIPGAV
RKTLDDAPGG GKRITFARPN GTFFHVVYGQ TEREVDVEGT TPPTATHDSQ GPFNTPFDKP
RKGQFQRYHD GPALVHKLGH YGYVCKEFET ELEFYTSNFN FVHSDILYLP QFPQMEVMSF
MHLDLGEEYT DHHTFFLQRA SPTVGSTYVH HTSFEVADFD TQLMGHHYLA KKGWKSVWGV
GRHILGSQIF DYWYDSSKFK IEHYTDGDVV NCHNPTRREP VGPLSVWGPE LPGDFGDNKA
//
