ID A0A364L9X9_9EURO Unreviewed; 537 AA.
AC A0A364L9X9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BHQ10_008523 {ECO:0000313|EMBL:RAO72511.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO72511.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO72511.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO72511.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:RAO72511.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MIKG01000019; RAO72511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364L9X9; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PIRSF; PIRSF000332; FMO; 4.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363}.
SQ SEQUENCE 537 AA; 60410 MW; EEFBAB72BBC67AB3 CRC64;
MADEQQQRFE GIRSVAVIGA GISGIMATKY LLQAGLDVTV FERNKKPGGV WLYDEKKAAE
PPYSATKPLE TAQALCPWYQ EANQQDGIVS AEDALRHAPP GACYEGLTNN FSLITIELKD
LPWLWEIPMT TPECPDNACE WTTHRNILQY VQNAASHVGL EDRVQYCTLV ERVKKEGGKW
QVTTGTLTST ASENTGEEMF QIRHRKREFD AIVVASGHYN TPRLPSIPGL LEWREAYPDR
VEHSKSYRHP QQYAGKVRVS SLRKKKIWLM NKKNQKNILL VGAGTSSTEI ARELGPFVKK
MYQSGRGSPF DLPLDFIPEN CHRIAEIESF GTLQNSIENA TTTEGHLPGE VTLKDGMILQ
DIDIVIVCTG YHFAYPFLPE LHADDESANV DVSQVLVTNG SCTLNLHKDM FYIPDPTLAF
VGISQFIATF SFFEFQAMFI ASVFSGKASL PKQEELRRIY EKRLAEKGDT RLMNGRQDEE
VSYVDELVAQ INVINPTKPV EGFSAKWHAA RDAGKLQKIR ARFAREKAER EAKETTV
//
