ID A0A0A2LB29_PENIT Unreviewed; 503 AA.
AC A0A0A2LB29;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=FAD linked oxidase, N-terminal {ECO:0000313|EMBL:KGO77307.1};
GN ORFNames=PITC_092670 {ECO:0000313|EMBL:KGO77307.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO77307.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO77307.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO77307.1,
RC ECO:0000313|Proteomes:UP000030104};
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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:KGO77307.1}.
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; JQGA01000203; KGO77307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2LB29; -.
DR STRING; 40296.A0A0A2LB29; -.
DR HOGENOM; CLU_018354_0_1_1; -.
DR OMA; KKAWDIY; -.
DR OrthoDB; 1068078at2759; -.
DR PhylomeDB; A0A0A2LB29; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF9; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..503
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001990956"
FT DOMAIN 71..241
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 503 AA; 53960 MW; D417FF1A7A9CBE66 CRC64;
MYQLKLEVIT AITAWAFTAA SLALPSGIDG GICPRGDADF EEFGKKLSGT AKVYHPGSSG
FADITTRWSA LAEPKVNIVV VPGTEQDVVE TVKFANMKDL PFLTYNGVHG ALVSLGKMDH
GVGISLSQLS SVKIAQDGKT ATMGGGTMSK VVTDQLWAAG KQTVTGTCEC VSLLGPALGG
GHGWLQGHHG LVSDQFVSMN VVLANGTLKQ IDYKSDLWWA MKGAGHNFGI VTSLTSKIYD
IQHSDWAIET ITFSGDKVEA AYDAANKYLL KNGTQPADLI NWSYWMNNAD LDATNPVIVF
YIIQEGVQAV DSIYTKPFHD LGPLSVVPQV GTYKDLGGWT GIALDSPPCQ NAGFANPRYP
IYLQSYNVAA QKKAWDIYAP AIRGSSAFNN SMFMFEGYSV GGVHAIPSSS SAFPFRSENI
LAAPLINYSP GDPAVAAEGA ALGQQLRNIL FEASGDKDIR AYVNYAHGDE TTNQLYGDSK
TRLLALKKKY DPTGKFSFYA PIA
//
