ID A0A319A785_ASPLB Unreviewed; 618 AA.
AC A0A319A785;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=FAD binding domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO96DRAFT_396254 {ECO:0000313|EMBL:PYH55075.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH55075.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH55075.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH55075.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; KZ821355; PYH55075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319A785; -.
DR OrthoDB; 2730557at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02979; PHOX_C; 1.
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 InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
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; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 15..381
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 410..567
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 618 AA; 69373 MW; 96760C11904AB497 CRC64;
MTIAPYPVGA FKSQRTDVLI VGAGPAGCMA AATLQRYGID FCLIDKRPTR TQTGHASAFQ
PRTQEILQTM NLLHDLDKRG HRLTETSFWM RDSTGALISN FTGAEVVHAT PYQYLFNTDQ
GMTEDVFEQY LNTKGQKIQR FMELVHYEHD LDPEWPLTAY IKNNASGAIE AWQTKYILGT
DGARSATRRA TGVQSSSQGG EDVWAVADVY VDTNFPDYRR RCAIRTPDGG CMLIPRKDEG
LRIFLQVDEK SQEHLDENGA SGQDALTGNS AFKLTQTVQS HINKVIHPYK MNITDIVWIS
QYRVAQRVVH HFSDPTKRVF LLGDACHTHS PKAGQGMNVS ISDAYNLTWK LALVMKGVAK
ASLLETYEQE RLWVAQQLIE FDALFARQFG QKDKLDSQNL RETWEMGHGF TSGCGYEYPA
NLLVNPDVRT SINNQAVEPL TPGKRLLPID LIRHIDGNHV RMLDIMPSNG RFHLFIFAGN
DLSSPTLQKL GNTLDSPHSP MSLFNLLPLE LMERFRHEDI TTASVPFTNK AYVLDLFLIH
SQNHLDVQLG NIPSPFSTKW PMNVYSDFDG AAQNQLGVPE DSGALVVVRP DGYIGLVTGL
DNVEDVTSYF DGFMHRRI
//
