ID   PPSB_ASPOR              Reviewed;        2429 AA.
AC   Q2UB00;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Reducing polyketide synthase ppsB {ECO:0000303|PubMed:32885554};
DE            EC=2.3.1.- {ECO:0000305|PubMed:32885554};
DE   AltName: Full=2,4'-dihydroxy-3'-methoxypropiophenone biosynthesis cluster protein B {ECO:0000303|PubMed:32885554};
GN   Name=ppsB {ECO:0000303|PubMed:32885554}; ORFNames=AO090102000166;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=32885554; DOI=10.1002/cbic.202000505;
RA   Kan E., Tomita H., Katsuyama Y., Maruyama J.I., Koyama Y., Ohnishi Y.;
RT   "Discovery of the 2,4'-dihydroxy-3'-methoxypropiophenone biosynthesis genes
RT   in Aspergillus oryzae.";
RL   ChemBioChem 22:203-211(2021).
CC   -!- FUNCTION: Reducing polyketide synthase; part of the gene cluster that
CC       mediates the biosynthesis of 2,4'-dihydroxy-3'-methoxypropiophenone
CC       (PubMed:32885554). The first step of the pathway is the conversion of
CC       acetate into acetyl-CoA by the acyl-CoA ligase ppsA (PubMed:32885554).
CC       Acetyl-CoA is then used as a starter unit by the polyketide synthase
CC       ppsB and condensed with 4 malonyl-CoA unit to produce the pentaketide
CC       backbone (PubMed:32885554). During polyketide extension, the polykedite
CC       chain is probably reduced and dehydrated by the KR and PT domains,
CC       respectively (Probable). O-methylation seems to be catalyzed by an
CC       unknown methyltransferase rather than by the CMeT domain of ppsB
CC       (Probable). Two hydroxylations and one further decarboxylation step
CC       catalyzed by yet unknown enzymes are then required to yield 4'-hydroxy-
CC       3'-methoxypropiophenone (Probable). PpsC functions as a carrier protein
CC       to transport 4'-hydroxy-3'-methoxypropiophenone to a specific cell
CC       compartment in which 4'-hydroxy-3'-methoxypropiophenone is hydroxylated
CC       to 2,4'-dihydroxy-3'-methoxypropiophenone by a still to be identified
CC       enzyme (PubMed:32885554). {ECO:0000269|PubMed:32885554,
CC       ECO:0000305|PubMed:32885554}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:32885554}.
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:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of 2,4'-dihydroxy-3'-
CC       methoxypropiophenone and 4'-hydroxy-3'-methoxypropiophenone.
CC       {ECO:0000269|PubMed:32885554}.
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DR   EMBL; AP007162; BAE61265.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UB00; -.
DR   SMR; Q2UB00; -.
DR   STRING; 510516.Q2UB00; -.
DR   EnsemblFungi; BAE61265; BAE61265; AO090102000166.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   OMA; GGFEGWW; -.
DR   Proteomes; UP000006564; Chromosome 4.
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   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; IPR013217; Methyltransf_12.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
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; PF08242; Methyltransf_12; 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; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..2429
FT                   /note="Reducing polyketide synthase ppsB"
FT                   /id="PRO_0000451834"
FT   DOMAIN          2350..2425
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          7..445
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          558..873
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          945..1227
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1409..2158
FT                   /note="Methyltransferase (CMeT) domain"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        177
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        652
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2385
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2429 AA;  266346 MW;  D60705D8D08BB96F CRC64;
     MKVDERVAII GTGCRFPGGS NSPHELWELL VNPRDVARKV PPDRFNIAAF HHPQMGHHGT
     TAAWESYFLD ENIQRFDASF FNISPTEAAA MDPQQRLLLE TVYESLDRAG LRLEELQGTQ
     TGVFCGLMRH DYHRLLTADM ETNPPYALAG TAGSVLANRV SYFFDWHGPS ITIDTACSSS
     LVAVHLACES LRKGECSLAI VGGSNLLLSP DPYIWESKMQ LLSPTNRCHM WDASADGFAC
     GEGVASVVLK RLTDALADGD HIECVIRATG VNSDGRSPGL TMPNSNAQSA LIMDTYARAG
     LHPKQNPHDR CQFFEAHGTG TKAGDPQEAA AIQDALFGCN MEENQPNNET VYVGSIKTII
     GHTAGAAGLA GVIRASLALQ NGVVPPNLHF NRVSDTVAPH TTHLEVPTRA VRWPELPSGV
     PRRVSVNSFG FGGTNAHAIL ESFDQASRHP STQVERVHQS QQALLPIVFS AASQSSLADL
     LEGYVQWLFD NPNVDLLGLA SSLLLRRSTL RYRKAFIAAS PDELRIKIQH ELKRNTTDAQ
     WAIMSPPKRE GGNCILGVFT GQGAQWPQMG LELIQNCPQA RMRLRELQQS LDDLPIEYRP
     GFTLLDELSA PESQSRLGET ALSLPLRTAL QIIQIDLLRA LGITFNAVVG HSSGEIAAVY
     AAGILNATDA IRVAYLRGFA VKHAASRGKM IAVNLTEHQA NAICSQPMWK GQVAVAAYNS
     PSNVTLSGDP ETMDELVWLL RSLERHTHPL NTDAAYHSHH MQPCAGPYLQ ALKSCNVGVS
     SPSSVQMFSS VYKGLVVNST DCALDSTYWC DNMLRPVLFS QAISTCLDQI PDINLIIEVG
     PHTALQGSIK HILHDTLSEG SVVPYIGLAH RGEDSIQSMA AAIGRLWAYL GMRDLKLQQY
     IQLFGPFRES CCVQSLPTYP FDHRTSYWAE PRLSQARLHC PIPPHPLLGV LSSECGRDEW
     RWRNYLHLEE IPWLTGHRIL SDISYPPMGY IAMAVEAAQA ASRSKPLQLV EIHSLIIERT
     ISIPVEGPGI ETLFKMDIES ADNDTMTGTF QCQISCGNEF QKCASGRVIL ALGEANPTVL
     PSKSKGMSIS YPMNVDKFYN QLQIVGGNVS DIFRGITELT RQEGGMQGVA NVPSHDQPTF
     HPVVMTTALQ VLWGAMMSDE GRLSALPLPV RIDSVTINPS CSHSGHVCLE ASITRTGSGR
     NGCGDVLVFN GQGDGIAQLE GIHLTLSKPK NSSDDQALAF GTTVWGPLNP DPSIGYPKNL
     PYNLSIQNLQ ARLAVLYLRD AQAGLTAQDR ERLVSHRRHY VAWMDSTLSK IRDGVHPHYP
     RDWLLGTIGE LDSQTTSHET LIHVTHIVGQ NLLQFLSGGE ETILLKLRDN NIDLLTRYYQ
     DDEAMRIMSD SLGKVVSQIV FRNPQLHVLE VGAGTGSATR AILSSIGRNY HSYTYTDISP
     AFFEGASAAF HTHEDRFIYK VLDVECDVTD QGFSMHSYDV VIASNVLHAT RSLRRTLMNI
     RKLIKPSGYL VLLEGTDPDR VPTPFIFGAF EGWWLGEDDG RSGGPLIRRE EWDVLLQCTG
     FGRCTSYTPT NQANLYGMSV IVSQPTDMPA IPVIEMDLLL VGGSTETTRQ IILDLKTILR
     DSFVQISSCL SVDDFTPGPG ISQLAILCLA ELDHHSEETR WQWQDMRLMM TAASCLLWVS
     PADDPHSGVS KGLLRSLALD SSSGLLQHLT VIDSTPIGAE MLATTLMNLV RTKQEGMGRP
     EIELGWGEGI LNIPRIVRDP TITQRLLASR SPCVFNLVDV REQAVCRLVS TEGSQKEKVD
     VYLTDPKNAT TSAAKLFSNE SIVQYQVHYC TQAALTITEK CSLFLIVGQN VFNGARQLAL
     SISHGSIIST PLSWAWDVPA SVSTDNEPKL LAAVAATILA FAIADLAGPS STLWVHEAQA
     MGPTFMDALV SAVSDRQDIK NLTLTTSQCG LSDTRVHFVH PHSSTKTLSS VLPRNVSSAV
     LFDDGRLSRR SRLVLPRCAN FRSFSDFFRP SSIIEEIDIQ SVATILNSAC AFVTRKGYEK
     GSSPRIISPR EQSSVDSLEV VNWRQPTWIE AQILPASSLV SLSPTMAYVV VNMNHKLRRL
     VLDFLVRQGA RHIVWVGEWS DEDFAWIAQL SRDEVHVAVV QMWAFLSSIS DLYDQLTSTR
     KAEIPISSLQ TYMPIGGIIY DGLKDSPQQA AENTLLLDEL CGNDATFFIL VGSLLGHIGF
     TDSNSFIGST TGVLSGVISR RRQRGYVGSV LYLGEQNAVE DITLSAGDIR EAFSEAILLG
     PPESTSNGEI LAGLRNSEKW ELVPKLSAWN ESKTLLESDD KSQSAGQGQA HDTDAVTQLK
     LATSVAEARE IILQLFKEKL RRKLGLSSDV PLRRETLLHE LGIDSLVAVD IHIWFARELG
     AKIPVVQIMG AGSIGSMVDE VVKRRNGFT