PKSF_ALTSO
ID PKSF_ALTSO Reviewed; 2260 AA.
AC Q2ABP6;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Reducing polyketide synthase pksF {ECO:0000303|PubMed:16642517};
DE Short=RD-PKS F {ECO:0000303|PubMed:16642517};
DE EC=2.3.1.- {ECO:0000269|PubMed:16642517};
DE AltName: Full=Aslaniol synthase {ECO:0000305|PubMed:16642517};
DE AltName: Full=Aslanipyrone synthase {ECO:0000305|PubMed:16642517};
GN Name=pksF {ECO:0000303|PubMed:16642517};
OS Alternaria solani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Porri.
OX NCBI_TaxID=48100;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, AND CATALYTIC
RP ACTIVITY.
RX PubMed=16642517; DOI=10.1002/cbic.200600034;
RA Kasahara K., Fujii I., Oikawa H., Ebizuka Y.;
RT "Expression of Alternaria solani PKSF generates a set of complex reduced-
RT type polyketides with different carbon-lengths and cyclization.";
RL ChemBioChem 7:920-924(2006).
CC -!- FUNCTION: Reducing polyketide synthase that catalyzes the formation of
CC a C22 intermediate attached to the ACP. Release by intramolecular
CC hydrolysis by the enolized delta-carbonyl would give the pyrone product
CC aslanipyrone (PubMed:16642517). Alternatively, KR-mediated reduction of
CC the beta-carbonyl of the C22 intermediate would form a beta-hydroxy
CC thioester intermediate, which could be a substrate for a further KS-
CC mediated condensation of an additional C2 unit to form a C24
CC intermediate, which cyclizes by aldol condensation followed by
CC decarboxylation to form aslaniol (PubMed:16642517). Neither
CC aslanipyrone, aslaniol, nor their derivatives have been detected in
CC A.solani, probably due to a low abundance and/or extensive post-PKS
CC modification. It is assumed that the branching point from C22 to C24 is
CC the result of KR activity on the C22 intermediate anchored to the ACP
CC (PubMed:16642517). {ECO:0000269|PubMed:16642517}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:Q9Y8A5};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:Q9Y8A5};
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; an enoylreductase (ER)
CC domain that reduces enoyl groups to alkyl group; 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 (Probable). The ER domain
CC was found to be much shorter than those of other fungal RD-PKSs, and in
CC its nucleotide-binding domain (G/AxGxxG), the second glycine is
CC replaced by a serine residue. This suggests that this domain is non-
CC functional and is consistent with the absence of reduction of the
CC double bonds formed by the DH domain in the PKSF products (Probable).
CC {ECO:0000305|PubMed:16642517}.
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DR EMBL; AB234233; BAE80697.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2ABP6; -.
DR SMR; Q2ABP6; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0009058; P: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; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR020806; PKS_PP-bd.
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; PF08240; ADH_N; 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; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 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 PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..2260
FT /note="Reducing polyketide synthase pksF"
FT /id="PRO_0000444929"
FT DOMAIN 2174..2251
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:16642517"
FT REGION 23..448
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16642517"
FT REGION 598..933
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16642517"
FT REGION 984..1281
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16642517"
FT REGION 1544..1859
FT /note="Enoylreductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16642517"
FT REGION 1882..2104
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16642517"
FT ACT_SITE 194
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 689
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1016
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2211
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2260 AA; 247331 MW; 5ACEC878A9F2D5F0 CRC64;
MDAFIDSEEV PMSSSSPNRV EPIAIVGFGF KFPQDITNAE SFWKLLIERR STMTEIPKNR
WNIDGFYKEH GHRPGTVKNR GGHFLADDPA RFDAPFFSIQ PAEAECMDPQ QRLLLETSYH
ALENAGIPMQ AAMGTRTSVH VGCLLQEYSQ ISQRDAQMPG DYRIVGSSGL AMLANRLSWF
YDFSGPSMTV DTACSGGLVA FHLACQELSA GSVDMSLVCG NNLCLLPDST ALLSSLNMMS
KDSVCYSFDE RASGYARGEG FGVLILKRLA TAIADGDTIR GVVRSTGCGQ DGNTPSITSP
SQSAQERLIR ETYARAGLDL GHTRYFEAHG TGTPVGDPCE AAAISNVFSC RTPKDPIFVG
ALKSNMGHPE GASGIAGVIK TLLVLEKGII PPNVYPERIN PAVAAAGPNL KFPLVPATWP
TDGIRRASVN SFGYGGTNAH VVLDDALSFL RDHGLSGRHC TEILHASEGA TKPAIFDALA
INGEDGSYST DTSACSEFFA DNTPPDSMDD HETAPKLFIL SAFDERATQR SISTFENWMR
NHANDENDRQ LLNDVAYTLA EKRTSFPWKS VCVALPNSLS QLSWSAPARA RQRVNLCFVF
TGQGAQWHGM GRELMIYPPF RDAMLRADRY FKSLGSAWSL IDELYLTSKE DSVIHQPELS
QPICTALQMA IHDLLTSWRV CASISVGHSS GEIAAAYASR AISQESAWMI AYFRGLAVAI
AQALNPSPGA MIAVQAPLKL GNTSWTSRMQ NIRPISSLSA CYNSPTSFTL SGSHSMLHQL
AITLKQANIE VHILKIDVAY HSHYMKPVAG VYEKLLRTIE PGEQVEAQPS FVSTVTGKNV
QQLNALRTSE YWQQNLCGSV KFSATLQSIC ARQDASTLFF VEIGPHSVLR SPLGDILKES
GRDVAIDYSS VLRRDRAADI TALECAGKLH TIGASIDITE VNKESEKSPR FLPSLPSYQF
EDKKKYWLEG RTSIQYRQTQ FVHHELLGSR TPDWNEHEAR WTNRILLDQS PYLHDHQING
LCLMPAAGML TMAIEATRQY YGHRAENASG YKLKDVTFTK AMTLSADARG TEIQLTLRPA
AAESRDVQPG SLWNQFSLFV HEDGGWHLCC KGYVAIEYDD RRESSGELAE SATAMEEKKQ
AFLAASQECR IAIDSADIYG AFGQAGLTYG PTFKGMRNVK WDQRNQATGT IGLRDWQRHA
KFSYSDPHFI HPAALDTILQ TTFPAYSIYA KDSSATTVPT GFSNAWFSVK LMRDPSDPQD
VVVHAKVAGR GFRNKLFSIT AAFANTQELC FYGDLETSTI GRNSPSADNT EVPRSLYRID
WQPAEFHRPT AVSPPSALSK SCIHIIYDDS EPLQSELMQA LRRTMSAQDD VGVALVTWSS
VSQHELDNAT CVFLPGLDGN LLRRMQEDGL ANIKSLLLKA STLIWITFQH QTIDQSPTEG
LVSGLVRTLA TESEDYRLVS VSLNPETGLD TVATNITKVA TALLEPQDDP EDEYCEIDGR
LCTPRVVDDA ELTVQALSTK DTAVSITKPW SELDSPKLTI GAAGILKTLH YEQTSIQMDE
LASDDVVIQV KAVGLNTRDA LVALGQVHDE SFGSEIAGVV VNTGSSHDAG FQIGDRVFGV
TRGGVAQLAR CKASQLQRVP DRMSFCEAAA YPVAFCTAYY VLTQYCGTNS GDSILVHDAA
SVLGQAIIKI AAIHGYTKIF ATVSSAGGAH FLENSLHVPK SNIFSTDSLD FQHGIRHLTN
GEGVAVVVGS EDHLQDSWPC IAPFGRFVGV GEKDVFHSTA NGSKEIVLPP TTKNIAFVSV
SFQDLAESYM FKDIFKHALM LIEDAQVTMA LPPTVFKQSE IEPALRRLTD VDVVEKIVIE
MDSDEVVEME PAQNSTKPLF RPDASYLIAG AFGGIGQSIA RWMVQHGAKL LILPSRSPVE
GTGSERDHFV QELKAQGAEV YAPVCDIADH DQLRKMLVSF SHLPAVKGCI QAAMVMRDSS
FAKMTIEQWH QSLAPKVDGS WNLHRLLPLG LDFFVMLSSS TGIMGSFGQS NYTVGNTYQD
TLAAHRMRHG QRAHALALSM VTGVGYVAQN DQVQALLRVR GMLEEVPMED IYNLLRFCCD
PDRVDASTVG SQIITPLTLP ADLRAMGIVA PLGSTRPIYH YLDTLPSRLS SDTASAEAKN
RPSYKLSEAT SLVQATDIVV EAIQTQLSSL LVVSKDDIDS QRAIYRYGVD SLVAVEMRNW
FSKAIGADVG TADIMSDISI WLLAVKVAGK SKFVRNELKE
