ID   A0A074X8R4_AURPU        Unreviewed;       446 AA.
AC   A0A074X8R4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Putative monooxygenase {ECO:0000313|EMBL:KEQ81743.1};
GN   ORFNames=M438DRAFT_279115 {ECO:0000313|EMBL:KEQ81743.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ81743.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ81743.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ81743.1,
RC   ECO:0000313|Proteomes:UP000030706};
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 paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; KL584990; KEQ81743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074X8R4; -.
DR   STRING; 1043002.A0A074X8R4; -.
DR   HOGENOM; CLU_009665_19_3_1; -.
DR   OrthoDB; 981595at2759; -.
DR   Proteomes; UP000030706; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase 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; MONOOXYGENASE; 1.
DR   PANTHER; PTHR13789:SF147; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G01950)-RELATED; 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.
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:0000313|EMBL:KEQ81743.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT   DOMAIN          8..376
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   446 AA;  48810 MW;  84CE78827738FAFA CRC64;
     MSKNVKDMHI CIAGSGMGGL ACALSLARQG FTKISVYEYA SSLGFVGAGI QLAPNMARIL
     DRLNVWKPIQ AEAVDLKDTS IRQGSSDAEL ANVQLQYVRE TYGYPHMVGH RSNLAGEMYN
     GCKDESANIT FHFSHSVQKV HSWSPGVRFE VKPRDGEAFD VECDVLLAAD GVKSNIRDQM
     LALLNIDAKV VDSGQAAYRI MLDRKDMEND PELLELIDGE RATRWIGERR HIIAYPVSNN
     TIYNLSTAQP DTNFAAAPSA TYTTKGSKKE MLETYADFCP KVQKMLNMVP EGEVCEWKLR
     VHAPLPTWVH GSMALVGDAC HPTLPHLAQG AAQAIEDGAV LGVVLSKVPD TSAESINKAL
     KVYQELRKSR AEGLVALAAA NGREMHLGDG AAKEARDAAF KAIREGREGA KVPDRWADAD
     VQKMIYGHDC WKDAEEQFET LFAAAA
//