ID   Q0CHX3_ASPTN            Unreviewed;       466 AA.
AC   Q0CHX3;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=ATEG_06711 {ECO:0000313|EMBL:EAU33255.1};
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:EAU33255.1, 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 paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; CH476602; EAU33255.1; -; Genomic_DNA.
DR   RefSeq; XP_001215889.1; XM_001215889.1.
DR   AlphaFoldDB; Q0CHX3; -.
DR   STRING; 341663.Q0CHX3; -.
DR   EnsemblFungi; EAU33255; EAU33255; ATEG_06711.
DR   GeneID; 4322133; -.
DR   VEuPathDB; FungiDB:ATEG_06711; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_009665_19_3_1; -.
DR   OMA; VMTYTIG; -.
DR   OrthoDB; 981595at2759; -.
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   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; PTHR13789:SF306; HYDROXYLASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 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   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          42..392
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   466 AA;  51210 MW;  90C632CAF2D456E3 CRC64;
     MAAMAEAVAS LKAPTYPSNC LEFLKTLNKN GTAPPPTAKL KLDIIVVGAG LGGLATAIAL
     QQSGHKVTIF EQTPELGEVG AGIQIPPNST RLLLKLGLGP YLEPYVTEPG SISFRRWQSG
     KTIGFTNLIP DFRKTFDAPY YVIHRADFHS AMYRRARDAG VQVKLASRVI DYDPQMPSIK
     LADGSSYEAD LIVAADGIKS VARGKLHSDL EKPLERPGFA AYRATVDVEK MKSDPDMAWL
     LEKPALNIWI GDKRHVMTYT IGAGKSFNMV LSHPDDTDPS TWNQLTALHD MRAEFTGWDP
     RLTKIIGLIK NTIKWPLLSG TPLSRWASGK IVILGDAAHA MLPYMSEGAA MAVEDGVALA
     RALTKIQARS DIPEALLIYE KVRIERTSQM QEASLLNGQL WHFPDGPLQQ ARDEAMLPET
     KGLPFTHSPN QWSDPATQMW CYGYDTEGEI DKVFAQRGNL CPKGLL
//