ID A0A074VSX3_9PEZI Unreviewed; 496 AA.
AC A0A074VSX3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KEQ63538.1};
GN ORFNames=M437DRAFT_74789 {ECO:0000313|EMBL:KEQ63538.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ63538.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ63538.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ63538.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KL584831; KEQ63538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VSX3; -.
DR STRING; 1043003.A0A074VSX3; -.
DR HOGENOM; CLU_006909_5_0_1; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000030672; 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; 3.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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:UP000030672}.
SQ SEQUENCE 496 AA; 56749 MW; 45414655E309ADF7 CRC64;
MTRKFSVKNV CIVGAGPTGL ACAKYLLAEK AFERIDIYEQ RSRVGGIWDY SPEDKTPDDL
PVPSVTPHAG LAKPKWLQSG TRKALGSRIE EEALFLSPLY DRLETNIPRT LMGFSDFDWP
QDSQLFPKHE TVTQYLEDYA ADIKHLIHFN TQVLDVNLAG AKPDGQDLWS VKTQKVQHKI
QEDPVERTYD AVVVANGHFA VPFIPQIKGM KEWAEQYPNA ISHSMYYKKP EDYTGLKTIV
VGSGASGIDI AMQLMQACKL PLIQSERSKG FLLSDPTPKK LEKEEIVEFI IQDRAVRFAD
GTVEKNIDSV LFCTGYFYSY PFLNNLDPPL VTTGTHVQNL YQHLIYRPRP TLCFPVLQQR
VIPFPMAEAQ SAVIARLWNN RISLPSVEDM KAWEDNLRNE TSEGKRDFHL LLFPKDANYI
NAMYDWSMSA ADADTKGKRP PHWGEKQYWM REKFPEIKKA FQDRGEGRRQ VRSLEELGFD
FEKMKKESAV EQKSLL
//
