ID   W4935_FUSPC             Reviewed;         250 AA.
AC   K3UFY2;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Thioesterase FPSE_09186 {ECO:0000303|PubMed:25412204};
DE            EC=3.1.-.- {ECO:0000305|PubMed:25412204};
DE   AltName: Full=W493 A and B biosynthesis cluster protein FPSE_09186 {ECO:0000303|PubMed:25412204};
GN   ORFNames=FPSE_09186;
OS   Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=1028729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096;
RX   PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA   Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA   Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT   "Comparative pathogenomics reveals horizontally acquired novel virulence
RT   genes in fungi infecting cereal hosts.";
RL   PLoS Pathog. 8:E1002952-E1002952(2012).
RN   [2]
RP   IDENTIFICATION, FUNCTION, AND PATHWAY.
RX   PubMed=25412204; DOI=10.1021/np500436r;
RA   Soerensen J.L., Sondergaard T.E., Covarelli L., Fuertes P.R., Hansen F.T.,
RA   Frandsen R.J., Saei W., Lukassen M.B., Wimmer R., Nielsen K.F.,
RA   Gardiner D.M., Giese H.;
RT   "Identification of the biosynthetic gene clusters for the lipopeptides
RT   fusaristatin A and W493 B in Fusarium graminearum and F.
RT   pseudograminearum.";
RL   J. Nat. Prod. 77:2619-2625(2014).
CC   -!- FUNCTION: Thioesterase; part of the gene cluster that mediates the
CC       biosynthesis of the lipopeptides W493 A and B (PubMed:25412204). W493 A
CC       and B consist of six amino acid residues D-allo-thr, L-Ala, D-Ala, L-
CC       Gln, D-Tyr, and L-Val/L-Ile linked to a 3-hydroxy-4-methyltetradecanoic
CC       acid polyketide chain (PubMed:25412204). The biosynthesis starts with
CC       formation of the linear polyketide chain by the highly reducing
CC       polyketide synthase PKS40 (PubMed:25412204). The gene cluster contains
CC       a putative acyl-CoA ligase (FPSE_09184) for formation of a CoA
CC       thioester polyketide. The thiol bond could be hydrolyzed by the
CC       putative thioesterase (FPSE_09186) and then accepted by the first T
CC       domain in module 1 of NRPS32 (PubMed:25412204). The second T domain is
CC       responsible for accepting a threonine, which is adenylated by the A
CC       domain and epimerized to the D-allo-threonine formed by the E domain.
CC       The five successive modules incorporate Ala, Ala, Gln, Tyr, and Val/Ile
CC       into the final product, which is released by cyclization
CC       (PubMed:25412204). {ECO:0000269|PubMed:25412204}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:25412204}.
CC   -!- SIMILARITY: Belongs to the AMT4 thioesterase family. {ECO:0000305}.
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DR   EMBL; AFNW01000306; EKJ70676.1; -; Genomic_DNA.
DR   RefSeq; XP_009260578.1; XM_009262303.1.
DR   AlphaFoldDB; K3UFY2; -.
DR   SMR; K3UFY2; -.
DR   EnsemblFungi; EKJ70676; EKJ70676; FPSE_09186.
DR   GeneID; 20367803; -.
DR   KEGG; fpu:FPSE_09186; -.
DR   HOGENOM; CLU_066049_0_0_1; -.
DR   InParanoid; K3UFY2; -.
DR   Proteomes; UP000007978; Chromosome 1.
DR   Proteomes; UP000007978; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..250
FT                   /note="Thioesterase FPSE_09186"
FT                   /id="PRO_0000445379"
SQ   SEQUENCE   250 AA;  27629 MW;  2471E0A17F0A89B4 CRC64;
     MIRQIQKRPA GSNANPLFLF HDASGTISNY LALGLLGRDV YAIADSRIKA KGDESLQDMS
     RRYYALIKST VAEGTILLGG WSLGGMTALQ VAWIFSRDPK VNVAGVLMID SPFPDYRHAL
     SLALESPPSE DGPASTRSDI EKAMLQTVTM LHKWKIPVWR REPQPHTVML CAGNDVDSDH
     VALSLVDQFR DSPTLGWNER AGPSVVNESY PIQGHHFSIF DPRNIDSVTK TIVTVTAAME
     MMAPEDDEDY