ID W3WVT1_PESFW Unreviewed; 438 AA.
AC W3WVT1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=PFICI_10027 {ECO:0000313|EMBL:ETS77965.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS77965.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KI912115; ETS77965.1; -; Genomic_DNA.
DR RefSeq; XP_007836799.1; XM_007838608.1.
DR AlphaFoldDB; W3WVT1; -.
DR STRING; 1229662.W3WVT1; -.
DR GeneID; 19275040; -.
DR KEGG; pfy:PFICI_10027; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_12_2_1; -.
DR InParanoid; W3WVT1; -.
DR OMA; WYHERIA; -.
DR OrthoDB; 2158278at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase 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; FAD-DEPENDENT MONOOXYGENASE ASQG-RELATED; 1.
DR PANTHER; PTHR47356:SF3; FAD-DEPENDENT MONOOXYGENASE SRDH; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT DOMAIN 7..344
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 438 AA; 48839 MW; 60E3C9C518E29E46 CRC64;
MSEHFRCIIV GGGPMGLITA HALTAAGMDW VLLEREDDIV VQDTPCVVMY PDTLRVMDQL
GLVDRLFRIK TTVDRTQTLT HDGASYNTTY PHDWSMENHG RGNWYFHQPQ LVSVLYEALS
ESDRARVKTC KEVTDIEAES ETIIVHCSDG TVEEGSLVIG ADGGHSIVRD MMRINALAED
PKAAVNATLP FAASYRVLWG TIPMAENMKS NEAWECHGKG YSSQMFFGRG RGWFFVYEKL
KKPTRGLRNY TEKDMYSCAA RLANLPMTNK LRLRDVYAVS HGCGMADLGE GLVRRFAWGR
TVLIGEAGNK QTSHLGLGLN SGVQDIVALT NTLSKLVQHH GERHELVETE AIHLALRKYD
AIRRGDALHG SRTSARAARL HSWNGRALRL YDRYFLPAGG SSKKNYDGTI GAIVSHGMLL
DSLPETDPQH GRMPWLHL
//
