ID   DEP5_FUSLA              Reviewed;        2371 AA.
AC   A0A0N0DCA3;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Reducing polyketide synthase DEP5 {ECO:0000303|PubMed:19737099};
DE            EC=2.3.1.- {ECO:0000305|PubMed:19737099};
DE   AltName: Full=Depudecin biosynthesis cluster protein 1 {ECO:0000303|PubMed:19737099};
GN   Name=DEP5 {ECO:0000303|PubMed:19737099}; ORFNames=FLAG1_09232;
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   -!- 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}.
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DR   EMBL; JXCE01000338; KPA37941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0DCA3; -.
DR   SMR; A0A0N0DCA3; -.
DR   EnsemblFungi; KPA37941; KPA37941; FLAG1_09232.
DR   OrthoDB; 19161at2759; -.
DR   Proteomes; UP000037904; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.10.129.110; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 2.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW   Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..2371
FT                   /note="Reducing polyketide synthase DEP5"
FT                   /id="PRO_0000441944"
FT   DOMAIN          2286..2364
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          50..480
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          593..905
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          982..1158
FT                   /note="Dehydrogenase (DH) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1656..1964
FT                   /note="Enoyl reductase (ER) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1988..2163
FT                   /note="Ketoreductase (KR) domain"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        221
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        685
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1014
FT                   /note="For beta-hydroxyacyl dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2323
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2371 AA;  257215 MW;  C9EAEF7442392A38 CRC64;
     MPHFRESSSS SENGAIDHDL QHTFQRILSD DQYTKFSPNE PPLSQQLEPI AVVGMGCRLP
     GDVSSPSDFW KLMMEKKSGQ TPKVPSSRFN IDAHFHPDND RPGSFGVLGG YFINETLKEF
     DPAFFGITPV EATWMDPQQR KLLEVVYEAF ESAGLTLDQL SGSDTACFMA TFTADFQQMS
     FKEPSFRHSL AATGVDPGLL SNRVSHVFNL RGPSIVVNTA CSSSVYALHN ACNALRTHEC
     SAAVVGGSNL ILTVDQHMNT AKLGVMSPTS TCHTFNSYAN GYGRAEGVGA IYLKRLSDAV
     RDGDPIRGVI RSSATNNNGK APGVGITYPG FDGQRTVMRH AYQRSGLDPM LTGYFECHGT
     GTAIGDPLEV HAVSDIMNAA RKDADGPLNI GAVKTNIGHS EAASGLSAVI KSILMVERGI
     IPPTHGVTDL NPKIDWKGWK VHVPTDPIPM PKHLPVTRVS VNSFGYGGTN AHTIIESPKS
     LLSAPQNYKY SMSGPTIKAK QPRGATRRNR PHLLVFSAHD TGTLKRNAAA LGKVAPNYNL
     LDLSFTLANH RTRFQSRGMV VTTPATLQKT FTDGMPDFMV ASKNVTARNL GFVFTGQGAQ
     WAGMGQQLMT YYPTFLKAIR RMDLVLEDLD DAPSWTLEES LLENPETSRV GEAEFSQPLC
     TAVQVALVQL LRTWGIRPSV TLGHSSGEIA AAYAAGYLSE ADAILAAYYR GQVVKSIDTS
     GAMMAVGLGA EAVKSYLEPF QAEVVVACHN SPVGVTLSGN IDALKAIEET LKVDGVFARL
     VKTNSKAYHS HHMLPAVDKY ETLLRDNSQK GISGVSLNKV KMVSTVTNSV LSEDAVLDGK
     YWSANLVSPV LFNQAIQSAL TNKDMHIDTL IEIGPHSALS GPIRQIKAEL GADKVQYLPT
     LIRGSPCAGQ VLKLAGEFFL RDYPINLSQV SMLEETSPSG KILSRSGNLI VDLPPYQWDK
     TKKFWAESRE SKEHRSPRFP RHDVLGQLTI GGSLTEPTWR NVLRLKDLPW LRDHSLGGEA
     VFPAAGYLAM AMEATTQLNE MSGSPREIKS YVFRDVRIQQ ALVTPDDDDG IEVLFNMCPS
     RLATDNTATQ SWDFNASSVS PEGHLKNHMA GSIRINTSNK QRAVARPVPN LPQRASGKLW
     NQALKKVGFN YGPTFQDMDN ITFDGTSYCA QSMTNLKSTV MDNESRYVLH PAILDSCLQL
     MIVAIWAGRA GAMKFGAVPV NAEEIVIWRP TATQLDNSSA AKAFSWIDPR GQRLFNAHNQ
     LLAGDGEVLM EIKSMRCTAY EAAIPQTLET NVQPEPYSQM VSKPDVSFLN GDQRDLDLAD
     FIALAHFKNP ALRVLATDAS TASLLLSRIP ALGLTVATGS SGVSDMEAQF AGFDNASVLS
     LDLNDSLARQ SHEKLTRSFN LVISPGASMA TLRTVSELLL EGGQAVLQQD PTFSDQGLKD
     AGFSGLECFL GQSMFVTSSI QTRKPVLSTV QLLYHTNPTS HMSPLELQLR DAGIKTERLK
     LGDSCTPGAN IIALADLERP LIASMSEFDF LQIQKTLSEA SKILWVSCGG SLEGSPEYAM
     TRGLLRSLRS ERAALKATLV DFVPDDLDTN EFSLRTTSLA ATLFEGDQEL ETEYLARDGQ
     LLITRLVPFD IVNQRHGHNG DETQPHPFDA ETNLVGKVEA GKVVFEHSRS DPEPLQETEV
     EFRPLATGLT AEGRAIISGA SFETDFSHEA SGIVTRVGDA VNKVSIGDRV VAFSSNTFSN
     FQRVQECLVQ RLQDDEDSAT MASLPLYYGA ALYGLETLAR LRPGESVLIL PGLGLLGAAA
     IKVAQALGGH PSVAVRDSAE AEEVEVAFGV PRSQILVAYS PDRLMRCHEI DVVFSGSTTE
     PLLAEESWRN LPALSRFVSC SNSSASAAPS FASTAISRGA SYLSVNITGL FKKPHILGGL
     LERIIELFRS GLIPAPLLNV QNIAEINHIG SPSSQSLSST ETVLVHEKGT GTVDVVQSRP
     RLELRSDATY LLVGCLGGLG RSLTTWMMKR GACHFAFLSR SGTDSEQARI CVQELEARGA
     NVQVFRGDAA VKEDVEMAVA SISAHCPLRG VVNAAMVLRD GLFQNMSYDN WTTSIRPKVL
     GSKNLHEAIA SLDLDFFLMT SSVSGILGTP TQANYAAANS YMDALACLRR RQGKHACAVV
     LPMILGVGVV AQDLDLEVSL KRKGMYGIDE EALLSAFEAA IFEQQHSQDS QSNFDHLVVG
     LEATKLYNAR QEAEGDVDAF WTTDPRFSVL LDDMKQHSGD NQGDGEKGSI LSQVKAASDS
     PAQAISLVRD HFISKLARVL LLDQDEFDDD GSGRSIASYG IDSMIGAELR NWIFKELGLD
     VAFQQLLSPS LTISKFAELV CAAQGIVLDN E