ID   DEP1_FUSLA              Reviewed;         365 AA.
AC   A0A0N0DCA4;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Terpene cyclase DEP1 {ECO:0000250|UniProtKB:A0A455R4Z0};
DE            EC=5.4.99.- {ECO:0000250|UniProtKB:A0A455R4Z0};
DE   AltName: Full=Depudecin biosynthesis cluster protein 1 {ECO:0000303|PubMed:19737099};
GN   Name=DEP1 {ECO:0000303|PubMed:19737099}; ORFNames=FLAG1_09236;
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   -!- PATHWAY: Polyketide biosynthesis. {ECO:0000305|PubMed:28460114}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       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 membrane-bound ascI terpene cyclase family.
CC       {ECO:0000305}.
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DR   EMBL; JXCE01000338; KPA37945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0DCA4; -.
DR   EnsemblFungi; KPA37945; KPA37945; FLAG1_09236.
DR   OrthoDB; 1036136at2759; -.
DR   Proteomes; UP000037904; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Isomerase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..365
FT                   /note="Terpene cyclase DEP1"
FT                   /id="PRO_0000441936"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   365 AA;  40524 MW;  0C9FA17ED99A3A90 CRC64;
     MFQTSRSQLL YLSALGVWGL WGYAYFNGMF TRLDTITRTL HFPDNRPLRD SYTGLGPLDK
     QLTLLSVFYD VLTNSLSSGP RLLFFDINYA VACTNLWTLI ESRRRGVRSW FLKYPAWAMV
     LCNANGAAIV LPIYLYCVCR SKARLRDPVV PLHEAVALPI ITVVMLLQPL LIFAPAWFGY
     SGSETHHALI ALFQVAPVIV LGLYVGITSL LSYHFPATSL SSKEYKKWIS ASLILAGSVA
     SAVHIYTLTG ALFTRDSDVS LTRLFVPTGG FTDPIKTLVS NENLLAEYAA LLENLHLFSQ
     WDWIVVCLTS VVYAQLLLSR REGLKVNKPA VPYEAQEMIY LTIATVVLGP GGAGSFALAI
     REARI