ID A0A0D2ERZ3_9EURO Unreviewed; 557 AA.
AC A0A0D2ERZ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_09368 {ECO:0000313|EMBL:KIW50569.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW50569.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW50569.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW50569.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
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DR EMBL; KN847322; KIW50569.1; -; Genomic_DNA.
DR RefSeq; XP_013311153.1; XM_013455699.1.
DR AlphaFoldDB; A0A0D2ERZ3; -.
DR GeneID; 25331276; -.
DR HOGENOM; CLU_006937_8_0_1; -.
DR OrthoDB; 2041362at2759; -.
DR Proteomes; UP000054342; 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; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
SQ SEQUENCE 557 AA; 63217 MW; 1E334C0763294508 CRC64;
MPHITTELRD YGRRRSKTGP YADNLEVDAL VVGGGFGGVF CFYELRKAGF KTVIYEAGND
LGGTWRWNCY PGAMVDSEIP EYQLSIPETY KDWTWPSNYP TYEDLRAYFD HCDKVLDIKS
HTAFDSVVVE SQFNTDEGRW HVKTADGRTT KTKYLVIAAG FAAKRYVPDE FIGIDNFQGI
CHHSSFWPDL NIDVSDKKCC VIGTGASGVQ IVQKWGPNVR SLKVFQRTPN LAVPMRKRAL
TAEEQNELKP MYPELFSLRE KCFGGFLYTF SEKGTFEDTP AEREAFYKKL WADGGFRFWL
GNYKDYLFDA KANREAYNFW AKNVRYRVGD AKTRDLLAPL EPPHPFGVKR PCLELNYYEQ
FNRENVELVD IKNNPISQFT EKGIKLKDGT EHEFDVICIA TGFDIVTGGM TAMGLRNINS
TLLQDEWKKA AYTYLGTTIS GYPNMFHLYG PQGPTLLSNG PTTVEVQGRW IVDAIKQVER
QGLKYINPTA EAQAAYKKKI NALSDISLFP TTKSTYMGGS KPDKAFEQTN WAGGIPAYHA
EIRATLPDFV GFEKVKK
//
