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Database: UniProt
Entry: A0A179FTZ9_METCM
LinkDB: A0A179FTZ9_METCM
Original site: A0A179FTZ9_METCM 
ID   A0A179FTZ9_METCM        Unreviewed;       641 AA.
AC   A0A179FTZ9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Flavin-binding monooxygenase-like family protein {ECO:0000313|EMBL:OAQ68718.1};
GN   ORFNames=VFPPC_04918 {ECO:0000313|EMBL:OAQ68718.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ68718.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ68718.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ68718.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004721}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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:OAQ68718.1}.
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DR   EMBL; LSBJ02000003; OAQ68718.1; -; Genomic_DNA.
DR   RefSeq; XP_018145568.1; XM_018284182.1.
DR   AlphaFoldDB; A0A179FTZ9; -.
DR   GeneID; 28848176; -.
DR   KEGG; pchm:VFPPC_04918; -.
DR   OrthoDB; 49786at2759; -.
DR   Proteomes; UP000078397; Chromosome 3.
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; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR43098:SF2; FAD-BINDING MONOOXYGENASE AUSB-RELATED; 1.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:OAQ68718.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397}.
SQ   SEQUENCE   641 AA;  71293 MW;  A60C18DDA437BD62 CRC64;
     MTADGGSNEA VATPDMDLLK KYTEESEKRF REDGSAQYLE LAGSEVSKLA ELTKDPWVDH
     DVLNAQPPNL KDSDDIKVLI LGAGFGGLLH AVYQVEAGIN PSDIRMVDVA GGFGGTWYWN
     RYPGIMVDVE SSIYLPLLED TGYMPKNRFS YGPEIREYIV SIAEKWNLTD KGVFRTQARS
     YDWMEDEKRW KVVLTQDRGP KEQPLEMAVT AQFVVITGGV LNHPKTPKIP GLESFAGEMI
     HTGRWNYDIS GGSPVDWTLS KLKGKKVGIV GTGATAVQCV PQLAQWADQL YVFQRTPSSV
     DERDQASMIP EHWEKVTSKK GWWRARNENW CGMLAGHPME ENMVKDRWSE SKSYRYLAGG
     LHDKPYTMED IPELIGKAVA SDAPRAERVR QRVDTIVKDK ETADALKAWY PIWCKRPCFH
     DDYLPTFNLP HVSLVDTNAK GIESVNANGI VAGGKKYDLD VIIWSTGYRS PVTNMAEPSH
     NANISMSARG NTLAGLWAQH GATTLHGTVT PWMPNVILSG PSQTAACGNF MYTIENIARH
     GAYIISETIK RADDPKKATV EAVPEAAEAW ALQILTRATF QAPLAICGPS YFNEEGATRT
     MSTEERMKMM RGAICPLGVL KYVDTLQDWR ADGKMEGLKL A
//
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