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Database: UniProt
Entry: A0A0A2KDW4_PENEN
LinkDB: A0A0A2KDW4_PENEN
Original site: A0A0A2KDW4_PENEN 
ID   A0A0A2KDW4_PENEN        Unreviewed;       547 AA.
AC   A0A0A2KDW4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Monooxygenase, FAD-binding {ECO:0000313|EMBL:KGO60189.1};
GN   ORFNames=PEX2_033280 {ECO:0000313|EMBL:KGO60189.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO60189.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO60189.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO60189.1,
RC   ECO:0000313|Proteomes:UP000030143};
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KGO60189.1}.
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DR   EMBL; JQFZ01000080; KGO60189.1; -; Genomic_DNA.
DR   RefSeq; XP_016601255.1; XM_016740603.1.
DR   AlphaFoldDB; A0A0A2KDW4; -.
DR   STRING; 27334.A0A0A2KDW4; -.
DR   GeneID; 27676022; -.
DR   HOGENOM; CLU_009665_14_2_1; -.
DR   OrthoDB; 2786342at2759; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.120; -; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
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; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF21274; Rng_hyd_C; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:KGO60189.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   DOMAIN          14..369
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   547 AA;  59718 MW;  9040D9467061FC0B CRC64;
     MTVTKASDLL PDSIPVLIVG AGPIGLSLAI ELRLHGIEAA VIEKDLEIVD GHPKGRSNDL
     RTVEHYRRWG VSDKLRKFSW QPANPKQRLV ITESLIQKPL GSFPLLYGRD VEESNDLAAE
     PSFSVPQPVT MKFLQARALE LGASILRGWK VLSVRQDEDR VIAEIQSPSG EVHSITSAYA
     IGCDGPGSLV RKSAGIQQKG VEPIGQTLSF VVRAEGYRIS DLINSPAHDA LGMLFVLSPR
     VSSIISIPGK DDWGYSITVP DGKTLTEEEI LSIGREILGV KTNLKIVSRS SYKVFTRVSE
     SYQNGRLLIA GDASHLCPPT GGHNMNAGIG DAVNLGWKLA AVLKGWGGQK LLESYDLERR
     PVGELVSDAA MKNSYDLKKV AEIVEGLPSL EDASEGERLQ RGQLAYDLTY PEWNIVGVAL
     DQRYDRSPVI VRDSQPSEPY DGTKIWSHAT PGHRAPHVWL PDGSPLLDHL GEEFTLIDVE
     AVEKNVQEIL AAADRVGLPL KRLQLSAAVA RAKYAAEITI IRPDQYISWQ GSQSDNPALL
     VDIIRGV
//
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