ID A2Q7F3_ASPNC Unreviewed; 661 AA.
AC A2Q7F3;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Contig An01c0030, genomic contig {ECO:0000313|EMBL:CAK43437.1};
GN ORFNames=An01g00490 {ECO:0000313|EMBL:CAK43437.1};
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:CAK43437.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK43437.1, 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).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; AM269950; CAK43437.1; -; Genomic_DNA.
DR AlphaFoldDB; A2Q7F3; -.
DR EnsemblFungi; CAK43437; CAK43437; An01g00490.
DR VEuPathDB; FungiDB:An01g00490; -.
DR HOGENOM; CLU_018354_4_2_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878:SF176; FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 179..359
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 661 AA; 71966 MW; 06EB3CD93FBAC97C CRC64;
MKGYLSRGLA ISMVAPAAYA QATRAVASLS AAAATVTTSP SAAPPLFPWE KVQLTENALA
RVDTALNNQS LSRIFAFGAG DSANNSGTPQ HSCKVMPGDA TWPTESTWNI FDQLLGGGLL
KPAPLAASCY PDWPEYNTEQ CSEITSNWLD DSLHSIMAPL DEGRSCMPVG YNYTSTCTQG
GYPTYVVNVS TVAQIQLSVN FARNQNLRLI VKNTGHDFNG KPSGKGGLSI WTHRLKDKVF
YPSFTADGGY VGPAIKLGAG VQVSEAYDFG KELNLTVIGG GCLSVGVAGG FTLGGGHSPL
SSMYGMAADQ VLALEVVLAD GRFITATSKQ NSDVFWMLLG GGGSTIGVVT SMTVKAYPQL
PTTLVTFNWT MNDTPNAEAF WAAFQSYLDN FEDFVNAGTY GYYFLGSSGA EKGEASSGET
DYNFRMVSFV APNMTVPETQ NLLKPWFDTL NSLNVSFTPI YSHADNFYEV WEEDNFPLET
GGLDIYKLAS RLLPRNVFEN QDLRNRNFLA QKDAVDKGLF IMGFHISGKG SAVEPPTNIA
VLPAWRDALS HVIVATEWDF TSSWETVYNS SLFVTDWMDA LREISPDSGA YMNEGDLLEP
NFQQAFYGAN YPRLYELKQK YDPTGLFFAL TAVGSEDWEV QVTDPLPYSW NNNGRLCPRS
S
//
