ID G3XUL9_ASPNA Unreviewed; 393 AA.
AC G3XUL9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
DE Flags: Fragment;
GN ORFNames=ASPNIDRAFT_133343 {ECO:0000313|EMBL:EHA25847.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA25847.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA25847.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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:EHA25847.1}.
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DR EMBL; ACJE01000005; EHA25847.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XUL9; -.
DR STRING; 380704.G3XUL9; -.
DR HOGENOM; CLU_009665_6_3_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR46720:SF4; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 135..313
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHA25847.1"
FT NON_TER 393
FT /evidence="ECO:0000313|EMBL:EHA25847.1"
SQ SEQUENCE 393 AA; 44037 MW; 112BF6FB40C0C8A0 CRC64;
LSIKIYEQSP TAHELGAGIG FTACARKCMA LMDPRIAECV ARVATLNGEP EDPDYCMRFV
DGFRTYTEGD CVYVSGKVYK LYAGPRGFEG CHRGQFLEEV MKLMPEGAVE YSKRVEGYEY
LPSGRIQLGF SDGGRVECDL VLACDGIKSL IRTHLYPQSK PQYTHQFAFR GLVPMATAIK
KLGRYRALRQ HMHCGPRAHV LHFPVAKQQL MNVVAFVQDP NDWTHAGMTA PARKSEVVEA
FKEWGPFVRA VIDLLPEELD KWAVFDTFDS PVPKYAERRV ALVGDAAHAS SPHHGAGAGM
GVEDALALVT AIKRAREDVD RGTEVNGALE AAVRAYSRVR YERSQWLVRS SREVGWTYEW
MSEDVGADMD RAFADIKKRS YQVWHFDVEA MVA
//
