ID A0A0A2J9K6_PENEN Unreviewed; 438 AA.
AC A0A0A2J9K6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Monooxygenase, FAD-binding {ECO:0000313|EMBL:KGO52097.1};
GN ORFNames=PEX2_107560 {ECO:0000313|EMBL:KGO52097.1};
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:KGO52097.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO52097.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO52097.1,
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:KGO52097.1}.
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DR EMBL; JQFZ01000274; KGO52097.1; -; Genomic_DNA.
DR RefSeq; XP_016594866.1; XM_016748024.1.
DR AlphaFoldDB; A0A0A2J9K6; -.
DR STRING; 27334.A0A0A2J9K6; -.
DR GeneID; 27683445; -.
DR HOGENOM; CLU_009665_19_3_1; -.
DR OrthoDB; 981595at2759; -.
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:SF311; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G10180)-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000313|EMBL:KGO52097.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 2..323
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 438 AA; 48646 MW; C8470A5FEFBFDA10 CRC64;
MKVFIVGGGL GGLACAIACR REGIDVEILE RSPEVREVGA GIQIPPNGGR IMRDFGLLPQ
LIEHGSQVQQ VDFRRYKDGR LLRSMPFGDD ITEEFGVPWI IIHRVDYHRI LLDEAIRLGA
VLQLGAEVED IHTEQPAVLL TDGRCISADV VIGADGQMST VRRAVLGSPN SPVPTGDMAY
RATFSREQLE ALGDEKVNEL CEKIAVTSWL GPEKHTIFYP LRGGKEFNLV LMRPDNLSPD
SRKEQGDIHE MRESYADWDE TLQKLVSCVP SVYKWKLTHL SELESWSKGS VALLGDACHP
TLPYQAQGAA MAVEDGAVIG KLLGLLRAHY LNFTNSGGDP SISTRSSAQD LTANVLTLYE
KCRKARTARN VQGAIMNRKL FHIADGLLQM IRDFVLGYAG VTRKSDWTWL SSFRQGQTLG
LDVLEDCKKV FEEWRLTL
//
