ID A0A0A2L9Y7_PENIT Unreviewed; 480 AA.
AC A0A0A2L9Y7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Flavin monooxygenase FMO {ECO:0008006|Google:ProtNLM};
GN ORFNames=PITC_085730 {ECO:0000313|EMBL:KGO73435.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73435.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO73435.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73435.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO73435.1}.
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DR EMBL; JQGA01000827; KGO73435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L9Y7; -.
DR STRING; 40296.A0A0A2L9Y7; -.
DR HOGENOM; CLU_006909_5_3_1; -.
DR OMA; LYQHVVW; -.
DR OrthoDB; 2453855at2759; -.
DR PhylomeDB; A0A0A2L9Y7; -.
DR Proteomes; UP000030104; 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 PIRSF; PIRSF000332; FMO; 3.
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:UP000030104}.
FT REGION 67..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 54343 MW; E9BE1E400F907C07 CRC64;
MVPVKRVAVI GAGPAGAIAI DALAQEKTFD IIRVFERREG AGGCWIGDSS QPPTLRDFAS
LATRTADSPL PVPEKLPAQT PKSDQPRFTE SSVYPYLETN VDFLPMQFSQ EPFPEKRSEL
SISHHGPETP FRKWDVVRKY VESLVERRGY SDFVSYNTTV ELVEKVGTEW KVTLRKNGEK
SDYWWVEWFD AVVVASGHFW VPYIPQIEGL EAFEKTRPGS VIHSKHFRGR EKFADKRVVV
VGASVSAADI AVDLVETAKT PVHAITIGHA ANGYFGDEAF NHPKIQKHPS IERVSNRTVH
LTNGNCIKDV DHIVFGTGYS WTLPFLPSVS VRNNRVPDLY QHVVWQKDPT LLFIGAIAAG
LTFKVFEWQS VLAARLLAGR ATLPSAEVMQ KWEADRVKAR GDGVKFTLLF PDFEDYFETL
RRLAGEGEEG KGRKLPKFRR EWVRAFFEGH ERRKAMWKRL NSKSRALLNN ETIHKEVARL
//
