DEP5_ALTBR
ID DEP5_ALTBR Reviewed; 2376 AA.
AC D2E9X0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
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};
GN Synonyms=PKS9 {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], DISRUPTION PHENOTYPE, FUNCTION,
RP 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: Reducing polyketide synthase; part of the gene cluster that
CC mediates the biosynthesis of depudecin, a highly oxidized eleven-carbon
CC linear polyketide that acts as a histone deacetylase (HDAC) inhibitor
CC and makes a small contribution to pathogenesis (PubMed:19737099). 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}.
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:19737099}.
CC -!- INDUCTION: Expression is positively regulated by the depudecin
CC biosynthesis cluster-specific transcription activator DEP6
CC (PubMed:19737099). {ECO:0000269|PubMed:19737099}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of depudecin
CC (PubMed:19737099). Leads to a small but statistically significant
CC reduction of approximately 10% in lesion size on Brassica oleracea
CC (green cabbage) leaves (PubMed:19737099).
CC {ECO:0000269|PubMed:19737099}.
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DR EMBL; FJ977165; ACZ57548.1; -; Genomic_DNA.
DR AlphaFoldDB; D2E9X0; -.
DR SMR; D2E9X0; -.
DR PHI-base; PHI:2379; -.
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; 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..2376
FT /note="Reducing polyketide synthase DEP5"
FT /id="PRO_0000441943"
FT DOMAIN 2289..2368
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..906
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 983..1158
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1659..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 1015
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2327
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2376 AA; 259422 MW; FD469B9FFE2DF449 CRC64;
MPIFYESSSD ASDAAPEFDL RNACQRIVTD DEYVVSSSTE PPLSQQLEPI AVVGMGCRLP
GDVSSPSDFW RLMMEKRSGQ TPKVPSSRFN IDAHFHPDND RPGSFHVYGG YFINETLQEF
DPAFFGITPV EATWMDPQQR KLLEVVYEAF ESAGLTLDQL SGSDTACFMA TFTADFQQMS
FKEPSFRHSL AATGVDPGLL SNRVSHVFNL RGPSIVVNTA CSSSVYALHN ACNALRNHEC
SAAVVGGSNL ILTVDQHMNT AKLGVLSPTS TCHTFNSYAN GYGRAEGVGA IYLKRLSDAV
KDGDPIRGVI RSSATNNNGR APAVGITYPG FDGQRNVMMH AYQRSGLDPM LTGYFECHGT
GTAIGDPLEV HAVSDVMNAN RTEADGPLQM GAVKTNIGHS EAASGLSAVI KAILIAERNI
IPPTRGLTDP NPKIDWKGWQ INVPTESMTI PKHLPITRIS VNSFGYGGTN AHTIIESPNS
LLAFPQSYQY SMPGTTTKSK LARGAVKRNR PYLLVFSAHE IGALKRNATA YGRVAANYSL
LDLSYTLANH RTRFHSKGMV VTTPASLHED IVNGSPNLVL AHKKETATTL GFVFTGQGAQ
WARMGAQLMA YYPTFLTSIR RMDLALEDLN DAPSWTLEEV ILQDSATSCV GEAEFSQPLC
TAIQVALVQL FRLWGIQPSV TIGHSSGEIG AAFAAGYISE AEAIWIAYYR GQVVKNIDSV
GAMMAVGLGA EAVAPYVESY EPEVVIACHN SPSGVTLSGS VEILKSIEGT LQAEGIFARL
VKTNGKAYHS RHMLPAVERY ESLIGKARQA TTQKHVSSKT KMVSSVTNSV LADDAVLDEK
YWSANLVSPV LFNQAVQTAL KCKEVPEVDI LIEIGPHSAL SGPLRQIKTY LHADKLQYLP
TLVRGFPCAN QVLKLAGELF LRNYPLDLAR VTAIEEVYPS GKIIPRMGNL IVDLPPYQWD
KTKRYWAESR ESKEQRSPRF PRHDVLGQLT TGASLAEPTW RNILRIKDLP WLRDHSLGGE
AVFPAAGYLS MAMEAVTQIN EMTEKPCKIT SYVFRDIVIQ QALVTPDDDN GIEVLLNMHP
SRINTDDSGK QWWDFNVSSV SIEGHRKNHM AGSIAIRTSA RSGLARKVPN LPQRASGRLW
NHALKKVGFN YGPTFQDMDN ITFDGSTYCA HASTNVKTAV MNDESRHVLH PAIVDSCLQL
MIVAIWAGRA SAMQFGAVPV RAEEIVIWKP KATHLTEGAR ATMFSWIDPR GQRLFNAHSQ
LVAEDRTVLM EIKNMRCIAY EAAIPQKLEA PIQPRPYSQL VYKPDVLWVH NTQTHLDVAT
FVELAEFKTP GLRVLVTDLM VAQSLIAKFP GIPMTLANRD VKEAEAEADP SGVKKFSLMS
LDLTASLATQ SYEKLKNSFD VVIAPNILSN SLECIAELLV EGGQAVLGVN GSTIVHDLEK
AGLSGPVFSM KDTMFVTSKV RESDKPVSIL VQLIYRHNPT EDITRLRLHL EETGFRSRIS
KLGDPCPPGS NVIMLADLED PLVATMSEPE FQHLQTLLSD SANVLWVSCG DYLGAGIDPE
AAMTLGLLRT LRSERASLKA TFVDFVRTDL ASEEFLSRTT SLAIALFDDE KKLETEYIAR
DGQLLLSRLI PAEEVNKTHG KIGRETKPQP FDPKAELVGR IQAGKVVFET ALLDKPPLQQ
DEIEFRQLAT GFNLEDQAAI TGASFETDFS HETTGIVTKI GSAITKVSVG DKIVAFSASR
FSTYQRVAEC LVQVLGPEEP YTTIAGLPMY YGAALYGLET LARLQYQESV FILPGSGLLG
AAAIWIARAL HCLPYVVVRD SAEAEHVATT FSLPSAQILT EYRPEQLVDL DIDVVFSGSS
VEPAVAREAW RHTPAFSRFV NCTAAASTSP LDSIPASRGA SYLSVNFPRL FQKPRVLGTL
LERIMVLYRQ GSIPAPSITV RNITELNESI HSFVDSICDN KIVIAHQTSE GLVDIVESRP
RLSLPPDATY LLVGCLGGLG RSLTSWMMKH GARNFAFLSR SGMDSEQAAI LVNNLETRGA
NVQVFRGDAT VKEDVEEAVR SIPADRPLRG VVHAAMVLRD GLFQNMAYEN WTTSIRPKVL
GSKHLTEVVA DLNLDFFLMM SSVSGILGTP GQANYAAGNS YMDALARLRR SQGKPACAVV
LPMILGVGVV AQNDGLEDSL KRKGMYGIDE EALLDSFEAA IIEQRPQTCQ QNEALDHLIV
GLDPAGLHKA RQEAEGDVDA FWSADPRFSS LVHSMNVYGG GNQGGDGEAG SILTRLRAAG
TESPAKAVDL VRDHFIAKLA RILLVDEAEF GGDDNAERSI ASYGVDSMIG AELRNWIFKD
LGLDIAFQQL LSPSLTISKF SELVCGAQGI VVEQKV
