AF161_ALTAL
ID AF161_ALTAL Reviewed; 2349 AA.
AC V5Y0F7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Reducing polyketide synthase AFT16-1 {ECO:0000305};
DE Short=PKS AFT16-1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305};
DE AltName: Full=AF-toxin biosynthesis protein 16-1 {ECO:0000305};
GN Name=AFT16-1 {ECO:0000305};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NAF8;
RX PubMed=24611558; DOI=10.1111/nph.12754;
RA Takaoka S., Kurata M., Harimoto Y., Hatta R., Yamamoto M., Akimitsu K.,
RA Tsuge T.;
RT "Complex regulation of secondary metabolism controlling pathogenicity in
RT the phytopathogenic fungus Alternaria alternata.";
RL New Phytol. 202:1297-1309(2014).
RN [2]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=12019223; DOI=10.1093/genetics/161.1.59;
RA Hatta R., Ito K., Hosaki Y., Tanaka T., Tanaka A., Yamamoto M.,
RA Akimitsu K., Tsuge T.;
RT "A conditionally dispensable chromosome controls host-specific
RT pathogenicity in the fungal plant pathogen Alternaria alternata.";
RL Genetics 161:59-70(2002).
RN [3]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=15066029; DOI=10.1111/j.1365-2958.2004.04004.x;
RA Ito K., Tanaka T., Hatta R., Yamamoto M., Akimitsu K., Tsuge T.;
RT "Dissection of the host range of the fungal plant pathogen Alternaria
RT alternata by modification of secondary metabolism.";
RL Mol. Microbiol. 52:399-411(2004).
RN [4]
RP FUNCTION.
RC STRAIN=NAF8;
RX DOI=10.1007/s10327-004-0170-3;
RA Ruswandi S., Kitani K., Akimitsu K., Tsuge T., Shiraishi T., Yamamoto M.;
RT "Structural analysis of cosmid clone pcAFT-2 carrying AFT10-1 encoding an
RT acyl-CoA dehydrogenase involved in AF-toxin production in the strawberry
RT pathotype of Alternaria alternata.";
RL J. Gen. Plant Pathol. 71:107-116(2005).
RN [5]
RP FUNCTION.
RC STRAIN=NAF8;
RX PubMed=18986255; DOI=10.1094/mpmi-21-12-1591;
RA Miyamoto Y., Masunaka A., Tsuge T., Yamamoto M., Ohtani K., Fukumoto T.,
RA Gomi K., Peever T.L., Akimitsu K.;
RT "Functional analysis of a multicopy host-selective ACT-toxin biosynthesis
RT gene in the tangerine pathotype of Alternaria alternata using RNA
RT silencing.";
RL Mol. Plant Microbe Interact. 21:1591-1599(2008).
RN [6]
RP REVIEW ON HOST-SELECTIVE TOXINS.
RX PubMed=22846083; DOI=10.1111/j.1574-6976.2012.00350.x;
RA Tsuge T., Harimoto Y., Akimitsu K., Ohtani K., Kodama M., Akagi Y.,
RA Egusa M., Yamamoto M., Otani H.;
RT "Host-selective toxins produced by the plant pathogenic fungus Alternaria
RT alternata.";
RL FEMS Microbiol. Rev. 37:44-66(2013).
CC -!- FUNCTION: Reducing polyketide synthase; part of the gene clusters that
CC mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins
CC responsible for Alternaria black spot of strawberry disease by the
CC strawberry pathotype (Probable). AF-toxin I and III are valine
CC derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric
CC acid respectively, while AF II is an isoleucine derivative of 2-
CC hydroxy-valeric acid (PubMed:15066029, Ref.4, PubMed:22846083). These
CC derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic
CC acid (EDA) moiety (PubMed:15066029, Ref.4, PubMed:22846083). On
CC cellular level, AF-toxins affect plasma membrane of susceptible cells
CC and cause a sudden increase in loss of K(+) after a few minutes of
CC toxin treatment (PubMed:22846083). The aldo-keto reductase AFTS1
CC catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-
CC hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to an
CC alcohol (PubMed:15066029). The acyl-CoA ligase AFT1, the hydrolase AFT2
CC and the enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide
CC synthase AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450
CC monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in
CC the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural
CC moiety (PubMed:12019223, Ref.4, PubMed:18986255). The exact function of
CC each enzyme, and of additional enzymes identified within the AF-toxin
CC clusters have still to be determined (PubMed:12019223, Ref.4,
CC PubMed:18986255). {ECO:0000269|PubMed:12019223,
CC ECO:0000269|PubMed:15066029, ECO:0000269|PubMed:18986255,
CC ECO:0000269|Ref.4, ECO:0000303|PubMed:22846083,
CC ECO:0000305|PubMed:24611558}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a ketoreductase (KR)
CC domain that catalyzes beta-ketoreduction steps; and an acyl-carrier
CC protein (ACP) that serves as the tether of the growing and completed
CC polyketide via its phosphopantetheinyl arm. {ECO:0000305}.
CC -!- MISCELLANEOUS: Gene clusters encoding host-selective toxins (HSTs) are
CC localized on conditionally dispensable chromosomes (CDCs), also called
CC supernumerary chromosomes, where they are present in multiple copies
CC (PubMed:12019223). The CDCs are not essential for saprophytic growth
CC but controls host-selective pathogenicity (PubMed:12019223).
CC {ECO:0000269|PubMed:12019223}.
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DR EMBL; AB872925; BAO10621.1; -; Genomic_DNA.
DR AlphaFoldDB; V5Y0F7; -.
DR SMR; V5Y0F7; -.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
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 Gene3D; 3.40.50.150; -; 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; 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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
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 3: Inferred from homology;
KW Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Transferase; Virulence.
FT CHAIN 1..2349
FT /note="Reducing polyketide synthase AFT16-1"
FT /id="PRO_0000444854"
FT DOMAIN 2273..2347
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..465
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 37..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..888
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 958..1263
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1976..2164
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2307
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2349 AA; 257802 MW; E3C6224E1562483E CRC64;
MNGKSRDNGH DGKRQPVVPA EPIAIVGTAM RLPGDATNPS KLWQLLRNPP SDLSRRPPSE
RFSSAGFFHE DPEHHGTSNS EQSYFLREDI RAFDAAFFSI APREAEAIDP QHRLLLEVVY
EALEAAGIPL EKTQGSDTAV YVGQMSNDYW DHLLRDLDSI PKYMATGTAR SVTANRLSYF
FDWHGPSMTI DTACSSSMVA LHEAVQVLRS GRAGMAVAAG CHLVLGPESY VIESKLRMIS
PTGTCKMWDA GADGYARAEG CAALILKTLS SALRDGDPIA ALIRETGVNQ DGRTRGITMP
SAQAQAALIR ETYLRAGLDP THPRDQPQLF EAHGTGTQAG DPIEAEAIHL AFFNDGVAHK
GTRERKEREK LLVGSIKTVV GHLEATAGLA GILKGIAAMN HRMVPPNLWF RTLNQRIAPF
YRDFRVPTVL EEWPMTGFDG TLRCSVNSFG FGGTNAHTIL ESYEPQLVTA TKMPREISFI
TPLTFSAASA ASLVAVVDSY RRHLASKQDI SLADLAFTLQ SRRSALPYRI AFSGTDITSL
IKQMSESVDS VKGTANVSIG TLNQQGKLEG GPPKLLGVFT GQGAQWPGMG RELLKSSKVF
SDAIIKMEDS LATLPDPPSW SLVDQFKAKA SPSSSEEATV AQPVSLALQI GLVDLLRASG
VEFDSVVAHS SGEIAAAYTT GLISAHDAIR IAYYRGKYSA LATEGGGMMA VGMSFAEAEA
FCNQEQLRGR VTAAASNSPK STTLSGRLST LKEAASLLGN TFHRFLKVDK AYHSDAMLPC
CKPFQAILEK CDIKVHKPND VLWVSSVREG QQPRSFADLL SGPYWVETLH KPVLFSQALT
RVLQMRSFDA TLEIGPHPAL RGPSLQTHAD ISLEKGKVLL YKGVLERFKH DGEAFSSCLG
FLWQHFGWAH FEAYRSTSLT TDVPRVLDQL PTYPWNHESL YWTESSNSYR FRYREAYHPL
LGFRSVDSHA MELRWKNVWS LREMPWLKGH VVQGQAVVPG VSYVTLALEA AAALGREGQE
TTRIELHDIN IHRAIIVEED EYSGTNVFVS VSRQNPDASC TRATFNIYAS TNHEKEPFHV
CSGDILLSHF AKDSGIQALG EFVVSTVYKD MSSVEPSLFY SEMKEVGLCW KEPFLSDSMY
RSHHRSVLSA TRSTADAHDG QLLLSPVLLD IGFQGALVGF ASPGDGRLWN PYLPTHIDRC
TFDLENLKLN KPCYDEVYFS SAVMGSTLPD LSTTATFTCD VYGFYAIDGN PFVQVEGLKF
SCMYPAQETN DREMFANETW MPASPLDMEL QPYDAQKHMG NLGAVVENLS HCDPRMKILH
ISDGESLVVP ILESLQGAFA RLDIADSSQS PALRHVEEVK ELFPKDSKRI WSSDLNLTKL
TSSPAIAENS YDLIICAQTI ETGDDVESRC SKLRKLLKLG GSIILSTSPG TSCNLPLQRC
GFTGVELELS VGPESRLILT RAKDDTSKTL ETPLDDLDAC TGEVIVIGGH QPEIQAIVDT
FQKDVAGKLS KMTLLESLSD LETYGIPTDA TVLCLADLHD DTLRNLAEGT LGGMKLLFET
ARRVLWVTQG RRNQNPFASM MVGLGRCIIS ESPLLNLQFL DIEDPLSDPV THKTISECFI
RLISLTTTGD FNVVRSWNQE PEMVLSQGKL LIPRIRPLPA LNDRLNCQNR IIKKPLIAGD
GTSVELTRSG AFYAAQEYDD YSAGRRITIS HSVSLPIELP GQMKGYLGLG TMSSGERVVV
ISPNNRNIQS AEECAFAVHF QPRGNEADTL ALIASAIFIR MAWEHTSDYV VLHQPSQSVY
RLGTQMAEDA KSKLYFSVSG RNDLEKHANV VSIPSMATRQ SLRNLMPGQV GAFIHVPGLA
GAGDRVSADR MIRAMSTTCK IFHLATAAAS SQNKSIDIRL SFNWKKACRI LVQSVEDVAK
FGNSNMLAEN QPVKCIGIAE ISGTPFSYDA ARIIDWTKDS RLKVNIQSKN PTKHFSPNKT
YLLVGLTGDL GRSLAQWMVR CGAQHIVLTS RSPRVPDSWL QACREISPQA QVRVFKMDVT
DEADVRSVCH SICKSMPPIG GVANAAMVMD DCLFHKLQLA SFNRVVEPKV VGSMILDKIF
HDVDLDFFIM FSSISCIVGN RGQSSYSAAN LAETTIASGR RSRGLSASTL ALGMVVGVGY
VARANLPTEA IKDNVRMQNG IPLGETDVHT AFFEAMLLGK ESSRLIPELI TGLKSIGSED
VELPLWHENP RFSHLSLLEG LDDVSLDSKK SSQGKVSVRE QLRQSTMPQE PFEILSGSLK
QKLKVMLKID KQEISDEVAL VQMGIDSLSA VEIRSWFAKE VGVDLPVLKI LNGASIRGLC
LEAIGQWKK
