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Database: UniProt
Entry: A0A0A2IIR3_PENEN
LinkDB: A0A0A2IIR3_PENEN
Original site: A0A0A2IIR3_PENEN 
ID   A0A0A2IIR3_PENEN        Unreviewed;       448 AA.
AC   A0A0A2IIR3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Monooxygenase, FAD-binding {ECO:0000313|EMBL:KGO56378.1};
GN   ORFNames=PEX2_079850 {ECO:0000313|EMBL:KGO56378.1};
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:KGO56378.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO56378.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO56378.1,
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   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:KGO56378.1}.
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DR   EMBL; JQFZ01000170; KGO56378.1; -; Genomic_DNA.
DR   RefSeq; XP_016598173.1; XM_016745255.1.
DR   AlphaFoldDB; A0A0A2IIR3; -.
DR   STRING; 27334.A0A0A2IIR3; -.
DR   GeneID; 27680675; -.
DR   HOGENOM; CLU_009665_18_0_1; -.
DR   OrthoDB; 2163350at2759; -.
DR   PhylomeDB; A0A0A2IIR3; -.
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; 3.50.50.60; 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:SF261; SALICYLATE HYDROXYLASE_MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13860)-RELATED; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-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:KGO56378.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT   DOMAIN          150..355
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   448 AA;  49128 MW;  C1B7933CA36D9C77 CRC64;
     MKIAIIGAGI AGCAAYLELQ KHLPQPSKSD ESHEVIIYEA YNTSPSITAN ERKEDHTHSS
     TLIVGGGLGV APNGLNVLKR LDKELLKDVV RGGASLDDNT NNNNNRPPHM LATSRHSLWT
     ALRGRIPDHH IIHKRVTQVI ARSDGRNSIR FADNSPIVEA DLVIGADGVR GIAKRALFPD
     AKEDPYPPHY EGLVGVGGFI PAADVKDLVE PGSMNFVFGG NGFFGYFFSE SSVSAGKRDS
     PYHVSEPGDS LAWWSTYEIE ECPDRKTLDM VDVTRQLRER HAYWKEPVVK KVIQSLQVEN
     MYPTWTLPAL PTWERDGVVL VGDAAHALPS SSGQGSSQAL EDVEALALFL AHYLHALPDE
     VTPKAQKNAI KAAASQYVSL RQPHVNAILE SAQKTQNSKR EMGILKEYSM YAMMKIMGLF
     PGFLANQIRA AAEYNIADDV ARIIASDD
//
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