ID A0A0A2KAA0_PENEN Unreviewed; 515 AA.
AC A0A0A2KAA0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Monooxygenase, FAD-binding {ECO:0000313|EMBL:KGO61280.1};
GN ORFNames=PEX2_081340 {ECO:0000313|EMBL:KGO61280.1};
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:KGO61280.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO61280.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO61280.1,
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 -!- 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:KGO61280.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQFZ01000049; KGO61280.1; -; Genomic_DNA.
DR RefSeq; XP_016602163.1; XM_016745404.1.
DR AlphaFoldDB; A0A0A2KAA0; -.
DR STRING; 27334.A0A0A2KAA0; -.
DR GeneID; 27680824; -.
DR HOGENOM; CLU_009665_19_1_1; -.
DR OrthoDB; 2678872at2759; -.
DR PhylomeDB; A0A0A2KAA0; -.
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:SF315; FAD-DEPENDENT MONOOXYGENASE MDPD; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 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:KGO61280.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 43..392
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57695 MW; F2F392F39BE97E94 CRC64;
MGETTAPAAQ KFYTVGDKDE FDPEKWKSST PNELPKRDPE THVKVLIVGA GFAGLMTALE
CWRKGHNVVG ILERNHGPNY SGDLIIIQPS AIAVFRHWPD MLRELEEDKV TAPTYYYRHT
SELIYGPSEP SYNDPEHLEE RENFPYVGPV QIRKKFYTML LRQVAKIGIK VDYGQRVDQY
FEDEQAGVGG VVMGDGSVRV ADIVVAADAF KSRSELLIAG KHMPTQSSGM SVYRVSFPAH
LAMQDEEVRK RWEGVTANEF WLGAGMHIGL YVSPDLVAFG ITPRDEFLVE GSAKAKESWD
PDVDPEEVIE LLRRLPGWHP AVEALIRATP RGSLIHWPLL WRNLRPEWTS RGGRVVQVGD
CAHSTIPASV SGGTLALEDA ITLASSLQVA SHGGPSGAPL GAKVYNLLRY QRVSCTQKMA
FVNSQLLNAT SDWDAIMKDR KTVRLRFPKW VFNHDPEAYV YEKYGQAFAH LVTGAKFENT
NFPPGHKFVP WTIEDVYKDI GEGKKIEQLL DGDWS
//
