PKS19_PHANO
ID PKS19_PHANO Reviewed; 1763 AA.
AC A0A0H4ADX3; Q0TX07;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Non-reducing polyketide synthase PKS19 {ECO:0000303|PubMed:26025896};
DE Short=NR-PKS PKS19 {ECO:0000303|PubMed:26025896};
DE EC=2.3.1.- {ECO:0000305|PubMed:26025896};
DE AltName: Full=Alternariol synthase {ECO:0000303|PubMed:26025896};
DE Short=AOH synthase {ECO:0000303|PubMed:26025896};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DOMAIN, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=26025896; DOI=10.1128/aem.00278-15;
RA Chooi Y.H., Muria-Gonzalez M.J., Mead O.L., Solomon P.S.;
RT "SnPKS19 encodes the polyketide synthase for alternariol mycotoxin
RT biosynthesis in the wheat pathogen Parastagonospora nodorum.";
RL Appl. Environ. Microbiol. 81:5309-5317(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Non-reducing polyketide synthase that mediates the
CC biosynthesis of alternariol (AOH), a micotoxin that seems not to be
CC involved in virulence and oxidative stress tolerance (PubMed:26025896).
CC PKS19 alone is sufficient for AOH synthesis which is initiated by
CC priming with acetyl-CoA, followed by sequential condensations of 6
CC malonyl-CoA units (PubMed:26025896). {ECO:0000269|PubMed:26025896}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of alternariol
CC (PubMed:26025896). {ECO:0000269|PubMed:26025896}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT76667.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KP941080; AKN45693.1; -; mRNA.
DR EMBL; BK009264; DAA64872.1; -; Genomic_DNA.
DR EMBL; CH445365; EAT76667.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001805964.1; XM_001805912.1.
DR AlphaFoldDB; A0A0H4ADX3; -.
DR SMR; A0A0H4ADX3; -.
DR STRING; 13684.SNOT_15829; -.
DR GeneID; 5982894; -.
DR KEGG; pno:SNOG_15829; -.
DR eggNOG; KOG1202; Eukaryota.
DR OrthoDB; 68112at2759; -.
DR PHI-base; PHI:4776; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..1763
FT /note="Non-reducing polyketide synthase PKS19"
FT /id="PRO_0000438984"
FT DOMAIN 1689..1763
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:26025896"
FT REGION 20..261
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26025896"
FT REGION 387..825
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26025896"
FT REGION 922..1227
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26025896"
FT REGION 1334..1588
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26025896"
FT REGION 1619..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1726
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1763 AA; 193474 MW; C111DA1A28F973B7 CRC64;
MTRAKVIYFS GEIPQGDPEG DQRNLFRKLH LLSKERDYPI LASFLETVTW AMKEEHRRLV
RAQRDLLPTF ESILDLTDHV VELRKTSLGG AIERVLVLAF QLGSFIAYHE AHPLEYNFQA
SDTFLIARGP GMLSAAAVAL CPSLPMISSI SADITRVAFR FGLVVDQVCR SLEVSPDEIN
SAGAWIYCVY GVDPQKAHEA VTRFNAEKAY AETSMASVFN DDGKSVSIGG PPSTLKTLFT
ECDFFKRTKN VPMKKVQGMW HTGKVYGTEH VHQIIPKIHQ KHQLYLPLFS PVKGQPLEAA
SATDLLEQIM EEMLTQRIRW DRTIQNVTER LKQASPESTQ LIAIQPSQYV ESLIGQWRAD
MPTTTHTTED MMSAVMDLPL GNSRAKDAKS SKIAVVGMAC RFPGGADNAE KFWELLAQGR
DVHSPIPSDR FNIETHVDPA GKVPNTSKTP YGCFVDNPGL FDAMFFGMSP REAEQTDPMQ
RLALVTAYEA LEHSGYVHGR GIHARRVGTF YGQASDDYRE VNSGQDVGTY FIPGGCRAFG
PGRINYFFKF WGPSFSVDTA CSSSLAAIQA ACTSLWSGDV DMAITGGMNI ITNSDVYAGL
SNGHFLSPTG GCKTWDEGAD GYCRADGVGS VVLKRLEDAE ADNDNILGVV LAAATDHSAE
AVSITHPHDV AQAHLYNQVA RRAGIDPLAV GYVEMHGTGT QAGDSNEMKS VTNVFAPSTG
HIRDRDSPLH IGTVKSNMGH GEAAAGIMAF VKTMLVFQKG IIPPHIGIKT RFNPALPEDL
AKRNVVIPVT AAIWVRNSDR KRLAMVNNFG AAGGNTSIII EEAAPRPRTS EDVRKAQVIT
VSAKTANSLQ ENLKALVDYI EARSELSVAD LAYTLSARRN HYNYRVSVLA TSTAEAASLL
RPHIKTSLSQ TPHSGKQVPI AFAFTGQGTF YIGIGAQLYR DSHEFRKHID QLDSLVRRQN
FASFLPVVSG NVQPEDVSIV TMNLAIVCVE IALARLWESF GIKPSMVIGH SLGEYAALAV
AGVLSDSAAI FLVGTRARLL TSKCTSRTHG MLSVRASAAD IKHAGGDIPF EVSCINGPNE
TVLGGTLSNM EALSATLAAA GYRTFKLDLP HAYHTYQMDT IVDELVKQTE TVVCKKTTIP
IISPRFSRVM TSEDSIDVSY LIGATRETVD FAGALDDAWQ SGLVNESTIW LEMGHHPTCS
GFISRTLSST RMALPSLQRD TDNWLTLAKT LCSLYSAGIP IDWNEYHRPF EQALRLIDAP
TYAWTNKNYW IQYRGDWNLT KGRAMPKLDP TTTVVPVSKR FQTSSIHRLI SEQYTDGKAI
LSAESSITDP SLQGVVDGHA MNGYGVASSF LHAEMAFTLA KRVSDKSFAS AVSFGINVAD
FEYHEPVVKL INTSEPQPIL VSAEADLEKM EVHVKWFNPA KEIWYCHATV FYEDPSSWLS
TWSRSTKLIT SRIDALNDMA VTGKASKLTT DLAYSLFGKL VGYSKLYQTM QSVILNEDEA
MAEVQFPEDT GGSWTVPPHF IDGLISLSGF ILNGGTHFDN TNNFFITPSW KSMRFARPLT
PGGRYTAYVR MVPSDNHSFV GDVYVLQGSE IVGVVEAILF LQWPRVMLNR FFRPADVTAK
PAAKVPGKSE PSTRPHFKPH HVSRHKPTLT PRSPDEGSEN SDSSGVIISR PGGYSSSDQD
MEELPSPPAG MNDDMEKALA LVAEELAVDI GLLTDDALIA DLGLDSLMSL VMSQRLREEL
GLEIRDAFFL EITTIQDLKA LLR
