ID   USTP_USTVR              Reviewed;        2094 AA.
AC   A0A1B5L6A0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Non-reducing polyketide synthase ustP {ECO:0000303|PubMed:31050129};
DE            Short=NR-PKS ustB {ECO:0000303|PubMed:31050129};
DE            EC=2.3.1.- {ECO:0000269|PubMed:31050129};
DE   AltName: Full=Ustilaginoidins biosynthesis cluster protein P {ECO:0000303|PubMed:31050129};
GN   ORFNames=UVI_02036160;
OS   Ustilaginoidea virens (Rice false smut fungus) (Villosiclava virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Ustilaginoidea.
OX   NCBI_TaxID=1159556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IPU010;
RX   PubMed=27151791; DOI=10.1128/genomea.00306-16;
RA   Kumagai T., Ishii T., Terai G., Umemura M., Machida M., Asai K.;
RT   "Genome sequence of Ustilaginoidea virens IPU010, a rice pathogenic fungus
RT   causing false smut.";
RL   Genome Announc. 4:0-0(2016).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=31050129; DOI=10.1002/anie.201903759;
RA   Obermaier S., Thiele W., Fuertges L., Mueller M.;
RT   "Enantioselective phenol coupling by laccases in the biosynthesis of fungal
RT   dimeric naphthopyrones.";
RL   Angew. Chem. Int. Ed. 58:9125-9128(2019).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of ustilaginoidins, dimeric gamma-
CC       naphthopyrones isolated from different fungal species
CC       (PubMed:31050129). The first step in the biosynthesis of
CC       ustilaginoidins is the production of gamma-naphthopyrone precursor YWA1
CC       by the non-reducing polyketide synthase ustP, via condensation of one
CC       acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:31050129).
CC       YWA1 is then probably substrate of the ustZ to yield norrubrofusarin
CC       via a dehydration reaction (Probable). A key enzyme in the biosynthetic
CC       pathway is the laccase ustL, which catalyzes the oxidative dimerization
CC       of norrubrofusarin to ustilaginoidin A (PubMed:31050129). It can
CC       produce the M- and P-atropisomers in varying amounts, depending on the
CC       reaction conditions (PubMed:31050129). For the biosynthesis of 3-
CC       methylustilaginoid in derivatives such as chaetochromin A, a methylated
CC       derivative of YWA1 is required (Probable). The C-methylation is
CC       considered to be catalyzed by ustM, the phosphopantetheine attachment
CC       site of which indicates that it acts on the growing polyketide chain
CC       before release of the product (Probable). For the biosynthesis of
CC       chaetochromin A, it is assumed that saturation of the D2 double bond
CC       takes place before dimerization, and is probably catalyzed by an
CC       external reductase because no candidate gene was identified within the
CC       cluster (Probable). {ECO:0000269|PubMed:31050129,
CC       ECO:0000305|PubMed:31050129}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + H2O +
CC         YWA1; Xref=Rhea:RHEA:62652, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:133763;
CC         Evidence={ECO:0000269|PubMed:31050129};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653;
CC         Evidence={ECO:0000269|PubMed:31050129};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:31050129}.
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. {ECO:0000250|UniProtKB:Q5B0D0}.
CC   -!- DOMAIN: The C-terminal region is involved in Claisen-type cyclization
CC       of the second ring of naphthopyrone. {ECO:0000250|UniProtKB:Q03149}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BBTG02000019; GAO19112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B5L6A0; -.
DR   SMR; A0A1B5L6A0; -.
DR   Proteomes; UP000054053; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR001031; Thioesterase.
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; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53474; SSF53474; 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   1: Evidence at protein level;
KW   Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Transferase.
FT   CHAIN           1..2094
FT                   /note="Non-reducing polyketide synthase ustP"
FT                   /id="PRO_0000448919"
FT   DOMAIN          1689..1763
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          9..243
FT                   /note="N-terminal acylcarrier protein transacylase (SAT)
FT                   domain"
FT                   /evidence="ECO:0000255"
FT   REGION          357..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..816
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          914..1227
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1305..1629
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1644..1689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1762..1782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1844..2069
FT                   /note="Claisen cyclase domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q03149"
FT   COMPBIAS        1647..1669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        551
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1004
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1916
FT                   /note="For Claisen cyclase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q03149"
FT   MOD_RES         1723
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2094 AA;  226793 MW;  89FFCF4BEABB8742 CRC64;
     MANVFQIAVF GDLSVPYHSE LRRLFSEKRD YVLATLFTKS YYAVKSEISR LPPSQRAQFP
     FSSNIEELLN ADKESTTSNY ALDSFFFCLC QISSFVSHLN RSGTSYPRAS SSCLASRCIG
     LLAAVAISCS ENVYDLVSIA PEVVALAFRV GLLVQGKTKS VTLSSGNGAS CSTVIAGLDE
     PAASQLLNAY FDNKGAPALS RVYVSAVGSG TITLSGPPAQ LKEFLSHHSD LKAGKIQVGG
     LFHSPSLYTD ADVSGLVASA TAHLRGRVAR IPVILNGHEK QQELVGGETC QHLLEVVVSD
     ILRHQMRWDL AAERVIRAIR RSGCSAVELL PFVAGSVEGL SSVLRATMGI DRVDVPNTAG
     VDSSSRGSGH ADAEKQPARS KIAIIGFSGR YPEADDNEEF WELLAAGLDV HREIPKERFD
     PYLYFDPTCK KKNTSGVTKG CFVRNPDLFD SRFFSMSPRE ADQADPAQRF ALMTAYEAME
     MAGFVPDSTP SSQRSRVGVF YGTASDDYRE INAAQNVDTY FVPGGSRAFL PARINYHFRF
     SGPSFDVDTA CSSGLAAVHI ACNSLWAEDC DVAIAGGTNI LTNPDNWAGL DRAHFLSRTG
     NCNTFDDAAD GYCRSDTVAT VILKRLEDAL LDGDPVFGTI LGAYTNHSAE AVSMTRPHSG
     AQRAICTRIL RSSNVDCSEV SYVEMHGTGT QHGDATEMDS VLSVFAPDTT SRKSPLFIGS
     VKANVGHAES AAGISSLVKV LLMMQKNAIP RHVGIKTKLN RNFPKDLVQR NVHISLENRS
     WPRPDPRVVP HGRRVFINNF GAAGGNSSVL VEDAPVRPAP ERDDASWPVH AVAVSAKTQN
     SFKENIRALI AYLETRPDVS LGSLSYTTTA RRIHYSYRTA VVGSSVDEIR NALHDVAARE
     KHLSTAGGGP PIGFSFTGQG SQYLGMGKKL LSLPQFESLL AGLDGIVRLQ GFPSILDVVS
     GKAETPIEDM SPVKVQLAIA CLEMALGKFW IALGVVPQIV VGHSLGEYAA LNIAGVLSDA
     DTIHLVGTRA RLLEKACSMG SHSMLAVKAS AAEASSLRSS SHPDLDIACI NGPEDTVVAG
     SNSQIEAFKD LLNGRSVKST QVKVQFAFHS AQVEPMLEAF RQACGAVVVN EPSIPVISPL
     LGRVMKSASD IGPVGDYLAR HCRETVNFCE GVLSARNSGL IPDKMMWVEV GPHPICSNML
     RSTLGSSTQT IPSLRRGEDD CKIFTPALAK LYDSGLAINW GEYHAGAQQT KQVLLLPSYR
     WELKSHWIPY TNDWCLTKGD APAPQLLALP EAAAAAAAAE RRLFTTSVQY ITAESYGAQE
     ASMTARTDVQ HPDFREVLLA HQVNGRPVCS SAVYADMAYT MFSRMLEKSS VPFDKSDLGI
     EVADMAADKS LILNDDPSPQ MLELKASVNW STRQGSFSMS SISSADGKPT AKHAKCSGFF
     TDKSRWKSEW KRRDFLVKSR IQELRSSVHD DSGSVHMIKT GMFYKLFTAL VDYRDSFKGC
     RELVMRSADL ESTAKVRFNT PAGTADKWKL PPHWLDSLGQ ITGFTMNGND EVDSKNQVYI
     NHGWDNMKIC GVLSDQTTYN TYLKMQPKDK GSYCGDVYIF NQDMDEVVAV YEGVTFAAVQ
     RKVLDLVLPK PKAAAQSGAA AAAAAAAPSQ RQQQQQQQQQ QQPAQPVAAS QESGMDDMPP
     TLVPSEKKDV PSEKLKVIIA EEVGASISDV QDDAELAPLG VDSLLALTIS DRMLEELGLR
     VDSSAFISCI TVAELVRHIL GSSTPSSDSG PATPSITPLQ EPDFGTSALS ERIESAFASV
     QVESDRCSDT TQYGDEKADA VTKFEIPPAT SVLLQGNPRT CTRKVWLFPD GSGSAASYMP
     LPDVDPAKVA IYGLSSPFIK HTATAKPCQF GEMTAAYVAE MRRRQPSGPY SVGGWSAGGL
     CAYDAAQRLV ADGETVDALI LIDSPNPIGL KELPPRLYNE LSRLNVFGAE PGAKVPEWLV
     PHFKLFADIL VTCKLRPWQA AKPLPAWALW ARNGVDENQT IERWPSDPEN MTWLLNRRTQ
     AILGCNGWDE LLGKKNITVG VVEGAHHFSM LKQPAVPQVS DFLRTIMEST GAGI