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Database: UniProt
Entry: G3Y8A6_ASPNA
LinkDB: G3Y8A6_ASPNA
Original site: G3Y8A6_ASPNA 
ID   G3Y8A6_ASPNA            Unreviewed;       874 AA.
AC   G3Y8A6;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=ASPNIDRAFT_129569 {ECO:0000313|EMBL:EHA21015.1};
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:EHA21015.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA21015.1, 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   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007801}.
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:EHA21015.1}.
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DR   EMBL; ACJE01000015; EHA21015.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3Y8A6; -.
DR   STRING; 380704.G3Y8A6; -.
DR   HOGENOM; CLU_009665_9_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   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.30.20; -; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR   InterPro; IPR038220; PHOX_C_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43004:SF4; FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF07976; Phe_hydrox_dim; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          300..668
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          693..850
FT                   /note="Phenol hydroxylase C-terminal dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07976"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHA21015.1"
FT   NON_TER         874
FT                   /evidence="ECO:0000313|EMBL:EHA21015.1"
SQ   SEQUENCE   874 AA;  95765 MW;  BF21B21EC20A3A0F CRC64;
     QFSLHGRTAL VTGGARGCGL AFARGLAQAG ANVAIFDRIP PEEGFLSIER EYGVRTAYYE
     VDVSSPDSLA TGFSAFQADF DNALDICVPC AGINRHQTFL EFNYADHQEL LGVNVLGLFH
     TAQLAARQMI ANGTKHGSIV LVASMASHVA VRSQLCSAYC GSKGAVRAMC PAIAKELAEY
     GIRVNSISPG YVRTEMTAAF PHLIEEWKSA AMNGRIAEPE DIMGACVFLA SDATILAQKW
     GYQLTRQSVR TPSLVTNYYN NTHPEATMNV SSPLQTQGIH TMSPSAINEG FPSPSTIPTT
     TVVVVGAGPS GLMLTNNLLR YGTPVILLDD RPTATSTGKA DGLQPKTIET LKQLRLSDEL
     LRNGAKVYDI CFWESTPQNP TLNRTSRQTH YPDHLVGASD PYILLAHQGM LEDVLIKDIE
     ERGGSVQRNS PFVSVSKTSD GSGELEVIYN DNTTNTQKPI RTKYLVGCDG ARSKVRDFIP
     GAQLEGEMSN ASWGVLDGII DTDFPDLWSK VAVRSHTAGS ILWIPRERGM TRLYVELSST
     DGERVDRAKA TPEYVMARAR EAMQPFRLEW KFIEWFGNYV VGQRVARRFS DPENQIFIAG
     DVCPFHPSFS HQCTDLNNKI QAGANTSMHD SVNLAWKLNL VSRGLAPASL LNTYSEERRK
     IANDLIAFDA GHVAAFEKGE TALARNFEEN IRFISGVGAE YDAGVVTKSP QSKVKGGIQP
     GTLTRPAKVT RYIDANPVDL QLDIPMMGQF RVVLFVADVV GGKGFLEGFC GADALEGVHS
     VAKESYKKCP RGLSDEDKYF PLERYTSVSE VVTYGLVTRS EKREFELGDL PELLQKSRWT
     VYLDDVEGEE GCTGEWIGEM EREQVGVMVV RPDG
//
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