ID Q0CV67_ASPTN Unreviewed; 635 AA.
AC Q0CV67;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=FAD monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATEG_02417 {ECO:0000313|EMBL:EAU37379.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU37379.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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; CH476596; EAU37379.1; -; Genomic_DNA.
DR RefSeq; XP_001211595.1; XM_001211595.1.
DR AlphaFoldDB; Q0CV67; -.
DR STRING; 341663.Q0CV67; -.
DR EnsemblFungi; EAU37379; EAU37379; ATEG_02417.
DR GeneID; 4316719; -.
DR VEuPathDB; FungiDB:ATEG_02417; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_3_1; -.
DR OMA; IMAYEPA; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000007963; 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:SF7; P-HYDROXYBENZOATE-M-HYDROXYLASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT DOMAIN 8..366
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 411..587
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 635 AA; 70904 MW; 38A0E30615FC0099 CRC64;
MAPSDNQYDI VIIGAGPVGI LLSLCMSRWG YKVKHIDNRP VPTATGRADG IQPRSTEILR
NLGLKRQIMA YHPAKVYDVA FWDPLPGGKG IHRTGSWPSC PRFIDTRYPF TTLVHQGKIE
RVFIDEIEKA GGTIERPWTI VGFKNDGLDK TYPVEVQLKC IDTNVIETVR TKYLFSGEGA
RSFVRQQLNI PIHHKDPIAY VWGVMDGVVR TNFPDIETKC TIHSDAGSIM VIPREDNMVR
LYVQIASSSD PDWNPRKTAT AEEVQATAKK ILAPYWIEWD RVEWYSVYPI GQGISERYTL
DERVFMGGDA CHTHSPKAGQ GMNTAFHDAL NMAWKLHAVE SGLAERSILS TYESERKDIA
ETLLNFDAKY AALFSKRRPT AGEVGEASHM VAKVGTDEDE FVKTFKSSCE FTSGYGVAYK
PNVFNWDESH PAQSPLFGVP GVKLKVGRAF TPTTVTRLAD ANFVDLEQEV PANGAFRIFI
FAGKQANTKK AISDLAANLE KERSFLSVHR RPDIADVSFF ERHQPHSKLF TICVIYAAEK
NQVDIDSVPK ILRDYHHHIY ADDIPDVRVP QAQFAAHEKL GFDPEKGGVV VTRPDSHVAC
TVQLAEGSGT VDALNAYFNA FSTKPIGQDA QQSRL
//