PSPB_PENSO
ID PSPB_PENSO Reviewed; 398 AA.
AC P0DUK2;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Type III polyketide synthase pspB {ECO:0000303|PubMed:31086874};
DE EC=2.3.1.- {ECO:0000269|PubMed:31086874};
DE AltName: Full=Soppiline biosynthesis cluster protein B {ECO:0000303|PubMed:31086874};
GN Name=pspB {ECO:0000303|PubMed:31086874};
OS Penicillium soppii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69789;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX PubMed=31086874; DOI=10.1039/c9ob00807a;
RA Kaneko A., Morishita Y., Tsukada K., Taniguchi T., Asai T.;
RT "Post-genomic approach based discovery of alkylresorcinols from a cricket-
RT associated fungus, Penicillium soppi.";
RL Org. Biomol. Chem. 17:5239-5243(2019).
CC -!- FUNCTION: Type III polyketide synthase; part of the gene cluster that
CC mediates the biosynthesis of the alkylresorcinols called soppilines
CC (PubMed:31086874). The biosynthesis starts with the HR-PKS pspA-
CC catalyzed carbon chain assembly through nine chain elongation cycles,
CC using acetyl CoA and malonyl CoA as a starter and extender units,
CC respectively, to produce the polyketide soppiline A (PubMed:31086874).
CC In the first round, the KR, DH, and CMeT domains work to produce 2-
CC methyl-2-butenyl thioester (PubMed:31086874). In rounds 2 to 5, the KR,
CC DH, and ER domains fully catalyze the reduction of the elongated beta-
CC ketothioester, resulting in the insertion of eight methylene units
CC (PubMed:31086874). The unusual Z,E,Z-triene motif is likely constructed
CC during rounds 6 to 8 (PubMed:31086874). Typically, the DH domain
CC introduces a double bond at an alpha,beta-position of an elongated
CC polyketide chain, with the dehydration of a beta-hydroxy group
CC (PubMed:31086874). The last extension cycle would be carried out with
CC L-oriented beta-ketoreduction by the KR domain to produce beta-hydroxy
CC carboxylic acid soppiline A (PubMed:31086874). The type III PKS pspB
CC intercepts the elongated polyketide chain at round 8 from the HR-PKS
CC pspA, followed by a tri-keto extension and decarboxylative aldol
CC cyclization to produce 1,3,5-trisubstituted alkylresorcinol soppiline B
CC (PubMed:31086874). Subsequently, the cytochrome P450 monooxygenase pspC
CC catalyzes three-step oxidations at the C-4 methyl group to carboxylic
CC acid to yield soppiline C (PubMed:31086874).
CC {ECO:0000269|PubMed:31086874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 22 H(+) + 11 malonyl-CoA + 12 NADPH + S-adenosyl-
CC L-methionine = 12 CO2 + 12 CoA + 8 H2O + 12 NADP(+) + S-adenosyl-L-
CC homocysteine + soppiline B; Xref=Rhea:RHEA:66940, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58349, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:167549; Evidence={ECO:0000269|PubMed:31086874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66941;
CC Evidence={ECO:0000269|PubMed:31086874};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31086874}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q2U852}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR AlphaFoldDB; P0DUK2; -.
DR SMR; P0DUK2; -.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR InterPro; IPR011141; Polyketide_synthase_type-III.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11877; PTHR11877; 1.
DR Pfam; PF02797; Chal_sti_synt_C; 1.
DR Pfam; PF00195; Chal_sti_synt_N; 1.
DR PIRSF; PIRSF000451; PKS_III; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 3: Inferred from homology;
KW Acyltransferase; Transferase.
FT CHAIN 1..398
FT /note="Type III polyketide synthase pspB"
FT /id="PRO_0000452730"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q94FV7,
FT ECO:0000255|PROSITE-ProRule:PRU10023"
FT BINDING 47..54
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT BINDING 47
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q2U852"
FT BINDING 214..215
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT BINDING 267
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q2U852"
FT BINDING 321..324
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q58VP7"
FT BINDING 321
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q2U852"
FT BINDING 324
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q2U852"
SQ SEQUENCE 398 AA; 43195 MW; 705C555ADCFDE52F CRC64;
MVLNHSPPPG LYITGLGSQY PPYLLGPEKL EEFAARFYDV ESPGLKKLLQ INRSSGIETR
SAIRSYESGF ATRPEAPTIS ELAEFYHQAG VDLTTQACKK ALRESQISPQ HVTHTIGVTC
TNQGNPGFDL LVNRKLGLSA NVDRMLLHGV GCAGGLAIMR AAAQIACGAS MRRKPVRILA
FACELCTPNV RHDLAFAEKA PNAENISIAG ALFSDAAAAF VLCNEYAMAE TEITPLFQLL
EWGNSLIPDT VEHMAFFADV DGYRTVLTRD VPQYTKHAIG PMFEKLLPSY QSQIQSSSGE
GVGEVAKSLG VSDFDWALHP GGEAIIEGAK QVLGLTEDQL QASREIYRTR GNSSSATVLI
VLDRLRSLGK REYVVATSFG PGLAIEMAML RRCEVDED
