DEP1_ALTBR
ID DEP1_ALTBR Reviewed; 369 AA.
AC D2E9W6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 20.
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};
OS Alternaria brassicicola (Dark leaf spot agent).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Brassicicola.
OX NCBI_TaxID=29001;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND PATHWAY.
RC STRAIN=MUCL 202097;
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).
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). The reducing polyketide
CC synthase DEP5 is the central enzyme in depudecin biosynthesis by
CC yielding the backbone polyketide chain (PubMed:19737099). The
CC monooxygenases DEP2 and DEP4, as well as the uncharacterized protein
CC DEP1, then act as tailoring enzymes to modify the intermediate
CC polyketide chain into depudecin (PubMed:19737099).
CC {ECO:0000269|PubMed:19737099}.
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:19737099}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the depudecin
CC biosynthesis cluster-specific transcription activator DEP6
CC (PubMed:19737099). {ECO:0000269|PubMed:19737099}.
CC -!- SIMILARITY: Belongs to the membrane-bound ascI terpene cyclase family.
CC {ECO:0000305}.
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DR EMBL; FJ977165; ACZ57550.1; -; Genomic_DNA.
DR AlphaFoldDB; D2E9W6; -.
DR PHI-base; PHI:2375; -.
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..369
FT /note="Terpene cyclase DEP1"
FT /id="PRO_0000441935"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 369 AA; 40287 MW; F9C801674A51DF92 CRC64;
MPQTSTTQFF YLSALGIWGL WVYAFFNGMF DRLDTITRTL HFPDGRPLRS KYTNIGPLDA
QLTLLSAFYD VLSNTLTSGP RLLFFDVNYV VACANLWVLI ESRRRGVRSW FLKYPAWAMV
LCNANGAAIV LPLYLYLVCC SKARLRDASV PKHEATALLV STVVILLQPL LIFVPAWAGR
GGSHLHHGCI ALFQVAPIGV SVFHLGLASI LPREASDSSP SSRKDSKKCI VASLVLAGTV
AAAVHSYTVV GALITRDGQA SLTRLFVPAH GFSDPIEVPL QPSGLPAEYM ALVENLHLFS
QWDWIVVALT SVLYSHLLLS LRDGAVRAKA NHWVSPVEAQ ELVYLTVATI ILGPGGAASF
ALAIRESRI