ID A0A0A2JVU3_PENEN Unreviewed; 811 AA.
AC A0A0A2JVU3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Monooxygenase, FAD-binding {ECO:0000313|EMBL:KGO59534.1};
GN ORFNames=PEX2_075140 {ECO:0000313|EMBL:KGO59534.1};
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:KGO59534.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO59534.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO59534.1,
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:KGO59534.1}.
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DR EMBL; JQFZ01000094; KGO59534.1; -; Genomic_DNA.
DR RefSeq; XP_016600704.1; XM_016744784.1.
DR AlphaFoldDB; A0A0A2JVU3; -.
DR STRING; 27334.A0A0A2JVU3; -.
DR GeneID; 27680204; -.
DR HOGENOM; CLU_009665_12_0_1; -.
DR OrthoDB; 2332834at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR47356:SF2; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47356; FAD-DEPENDENT MONOOXYGENASE ASQG-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 Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000313|EMBL:KGO59534.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 450..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 607..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 641..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 681..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..344
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 811 AA; 90628 MW; 5640A93A1C276693 CRC64;
MQPNPKFRVI IVGGSVAGLT LAHCLLKNNI DFVVLEASPE VAPEVGASLG LLANGGRILD
QLGVYDDVQA EVVSIEDAYF WAADGSLMLK SNSPDELNKR HGYPIAFLPR RTLLKILLKH
LGDRQDDVVP NKKVIRVDHY PSHVIVHCAD GSSYEGDMVV GADGVRSVVR QSMWDYMESQ
GLKSEVQKER STMSAEYNCV FGMSTATPGL DPKDIHRTFG KDWSFLTIAG KGNKSYWFLY
NKMDRTYYGS DIPRFNKADI DERVAPYLHR PVTDSVPFSE LYKRSTIRTF VALEEANFNH
WCIDRFACIG DSIHKMTPNI GQGGNSAIES SATLANHLAR LLQRSSPYQT EDINRCTQAW
QASRRDRVDK ICREAFNLTR LEAIASPKYR LMIYLIPYMK TKMIEKTSAT LVASPKLECA
PETVKALWCS IPYKTEKPAS EATETIWERV LWGMPFLGCF AVASATMGAI LTKVRQLMIP
YFIQGTWRST NGEVLDIRKA VYHIPFLDNL LRPMITCFLP SISGSDLQSR AQMISFLADL
GAVYGIWLLE SYRKANGWSE VAIPISICSV FQLKGIGLLA PIYYLLEYVR TPLSKLLPKN
MREVEPTGSI SLLAAMLIGH YFPTFASFTA PTLDSRRWWN AMWQIFPITV PLIQLPFALL
GKRLLPSTKA SPEEKSQNSM TSTRIAYGGF ALISALTFIY ARCSAPADAS LLSIFWPGFS
SHHLPVTSFQ EGIARFLQYD QVLSMGSGFF WLALRFREIK QSGGSVSWWK AIGSLVATIS
SFGPGTAFAL GWGWREELIH KLAISQGVCS E
//