ID   APMLB_ARTPE             Reviewed;         307 AA.
AC   P0CU85;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Thiohydrolase apmlB {ECO:0000303|PubMed:31180682};
DE            Short=TH {ECO:0000303|PubMed:31180682};
DE            EC=3.1.-.- {ECO:0000269|PubMed:31180682};
DE   AltName: Full=Phaeospelide A biosynthesis cluster protein apmlB {ECO:0000303|PubMed:31180682};
GN   Name=apmlB {ECO:0000303|PubMed:31180682};
OS   Arthrinium phaeospermum (Gymnosporium phaeospermum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Apiosporaceae; Arthrinium.
OX   NCBI_TaxID=112178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=Kemushi-1;
RX   PubMed=31180682; DOI=10.1021/acs.orglett.9b01674;
RA   Morishita Y., Zhang H., Taniguchi T., Mori K., Asai T.;
RT   "The discovery of fungal polyene macrolides via a postgenomic approach
RT   reveals a polyketide macrocyclization by trans-acting thioesterase in
RT   fungi.";
RL   Org. Lett. 21:4788-4792(2019).
CC   -!- FUNCTION: Thiohydrolase; part of the gene cluster that mediates the
CC       biosynthesis of phaeospelide A, a fungal polyene macrolide with a 34-
CC       membered macrolactone ring and an all-trans conjugated hexaene
CC       structure (PubMed:31180682). The HR-PKS ApmlA uses acetyl-CoA and
CC       malonyl-CoA as its starter and extender units, respectively, and
CC       provides the large carbon framework in phaeospelide via 16 cycles of
CC       polyketide chain elongation, which is the largest number identified in
CC       fungal iterative PKSs thus far (PubMed:31180682). During round 1, the
CC       KR domain reduces beta -ketone to an L-oriented hydroxy group, while
CC       during later rounds, it provides hydroxy groups in the D-configuration
CC       (PubMed:31180682). The characteristic conjugated hexaene moiety is
CC       built during the later rounds (10-15), when the KR and DH domains are
CC       at work but ER is off (PubMed:31180682). Phylogenetic analysis of the
CC       DH domain suggests that a polyene formation is programmed in the DH
CC       domain (PubMed:31180682). Finally, the mature ACP-tethered carbon chain
CC       is transferred to the serine residue of the thiohydrolase apmlB,
CC       followed by intramolecular macrolactonization, generating phaeospelide
CC       A (PubMed:31180682). When one elongation cycle during rounds 7-9 is
CC       skipped, phaeospelide B is biosynthesized instead (PubMed:31180682).
CC       {ECO:0000269|PubMed:31180682}.
CC   -!- SIMILARITY: Belongs to the polyketide transferase af380 family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0CU85; -.
DR   SMR; P0CU85; -.
DR   ESTHER; artpe-apmlb; Thiohydrolase.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..307
FT                   /note="Thiohydrolase apmlB"
FT                   /id="PRO_0000447827"
SQ   SEQUENCE   307 AA;  34413 MW;  323FDE97A2571623 CRC64;
     MGLSEKVEFK TLDGLVLRGF LYSARAKGPA IVMTPGFNFP VSLLYHEVAL GFQAAGITAL
     VYDPRSVGRS DGLPRSDINP AKQSEDFSDA ITFLKTKPVV DPKRIALWGY SLSAAAALMA
     AGLDPRVKLV VAVCPAPVPY NFEAPGKRRK YLDLAIRDRE SQARGKEPFY VQYIGDSEET
     ALFDYRKQRG MEELEYDEVV ENLTKIAPGF RNEVTIQTLR RLGSWSFADV PQRVGPTPVL
     QVFAVHEELE HIRKTQEAIW AGLTGPKERH TEDRGHMDVL TPDGHRFAHL VKVQVDFVLK
     NFAQRMR