DEP2_FUSLA
ID DEP2_FUSLA Reviewed; 521 AA.
AC A0A0N0DCA8;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=FAD-dependent monooxygenase DEP2 {ECO:0000303|PubMed:19737099};
DE EC=1.-.-.- {ECO:0000305|PubMed:19737099};
DE AltName: Full=Depudecin biosynthesis cluster protein 2 {ECO:0000303|PubMed:19737099};
DE Flags: Precursor;
GN Name=DEP2 {ECO:0000303|PubMed:19737099}; ORFNames=FLAG1_09235;
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059;
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=19737099; DOI=10.1094/mpmi-22-10-1258;
RA Wight W.D., Kim K.-H., Lawrence C.B., Walton J.D.;
RT "Biosynthesis and role in virulence of the histone deacetylase inhibitor
RT depudecin from Alternaria brassicicola.";
RL Mol. Plant Microbe Interact. 22:1258-1267(2009).
RN [3]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=28460114; DOI=10.1093/molbev/msx145;
RA Reynolds H., Slot J.C., Divon H.H., Lysoee E., Proctor R.H., Brown D.W.;
RT "Differential retention of gene functions in a secondary metabolite
RT cluster.";
RL Mol. Biol. Evol. 34:2002-2015(2017).
CC -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC depudecin, a highly oxidized eleven-carbon linear polyketide that acts
CC as a histone deacetylase (HDAC) inhibitor and makes a small
CC contribution to pathogenesis (PubMed:19737099, PubMed:28460114). The
CC reducing polyketide synthase DEP5 is the central enzyme in depudecin
CC biosynthesis by yielding the backbone polyketide chain
CC (PubMed:19737099). The monooxygenases DEP2 and DEP4, as well as the
CC uncharacterized protein DEP1, then act as tailoring enzymes to modify
CC the intermediate polyketide chain into depudecin (PubMed:19737099).
CC {ECO:0000269|PubMed:19737099, ECO:0000269|PubMed:28460114}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:28460114}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression correlates with the production of depudecin with
CC high levels on oat grain medium, and minimal levels on oat flower
CC medium and complete medium (PubMed:28460114).
CC {ECO:0000269|PubMed:28460114}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; JXCE01000338; KPA37944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0DCA8; -.
DR SMR; A0A0N0DCA8; -.
DR EnsemblFungi; KPA37944; KPA37944; FLAG1_09235.
DR OrthoDB; 462247at2759; -.
DR Proteomes; UP000037904; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..521
FT /note="FAD-dependent monooxygenase DEP2"
FT /id="PRO_0000441938"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 320..324
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 521 AA; 57890 MW; 0A8B755FCC718BAF CRC64;
MHDSPPFKVI IVGAGVTGLT LAHCLVKAGI DYALLDKGVV APGFGTTITL QPHGCRILHQ
LGCLDAVLAK CDVMGGASCR DPNGKIFTSN DFFGVVRKFA GYDTRTLDRQ VFLHELYELL
PDKSKVYEKA RVEEIIEENS TTRVILADGR EFAGDLVVGA DGVHSKVREI MWDKANAAHP
GMITVEEKRA MVTQYNAIVM ASSPVPGISA HDMEVTSNDN YSFLLLCQPD WISIIVHSKL
PDDQQCTWPT RRRYTETDME ELVSKIIERP VTGSVVFGEL WKRRLKAQMI SLEEGVLSHW
TFGRIALAGD AVHKVTPNSA LGGNTAMEDA VVIANTLHAL LAMHPNKKPS DVEVRDAMRE
KYQNTRVDRA RAIVKAGGDL TRQQAYDGWK AYIKQRWLTP IIGLDTLAQK IAGLCVTAPK
LAYVDFDERR GILGWQDTLA AEKERESKTQ VKVPIKQKKG LSWSTWNGGF EAIVPQILVL
WAGLWLAICF FHLVFSGNHV PGFGSEVARF FTVYNETWMH S
