PVHB_TALVA
ID PVHB_TALVA Reviewed; 371 AA.
AC A0A3Q9U4G3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Diels-Alderase pvhB {ECO:0000303|PubMed:30609896};
DE EC=5.5.1.- {ECO:0000269|PubMed:30609896};
DE AltName: Full=Varicidin biosynthesis cluster protein B {ECO:0000303|PubMed:30609896};
GN Name=pvhB {ECO:0000303|PubMed:30609896};
OS Talaromyces variabilis (Penicillium variabile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces.
OX NCBI_TaxID=28576;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=HXQ-H-1;
RX PubMed=30609896; DOI=10.1021/jacs.8b12010;
RA Tan D., Jamieson C.S., Ohashi M., Tang M.C., Houk K.N., Tang Y.;
RT "Genome-mined Diels-Alderase catalyzes formation of the cis-
RT octahydrodecalins of varicidin A and B.";
RL J. Am. Chem. Soc. 141:769-773(2019).
CC -!- FUNCTION: Diels-Alderase; part of the gene cluster that mediates the
CC biosynthesis of varicidin A, an antifungal natural product containing a
CC cis-octahydrodecalin core (PubMed:30609896). The PKS module of pvhA
CC together with the enoylreductase pvhC catalyze the formation of the
CC polyketide unit which is then conjugated to L-isoleucine by the
CC condensation domain of the NRPS module (PubMed:30609896). Activity of
CC the Dieckmann cyclase domain (RED) of pvhA results in release of an
CC acyclic tetramate (PubMed:30609896). The cytochrome P450 monooxygenase
CC pvhE then catalyzes the oxidation of the C21 methyl group to a to
CC carboxylate group (PubMed:30609896). The methyltransferase pvhD then
CC further methylates the pvhE product (PubMed:30609896). The Diels-
CC Alderase pvhB is able to catalyzes Diels-Alder cycloaddition using both
CC pvhE and pvhD products as substrates to form the decalin ring, yielding
CC varicidin B and A, respectively (PubMed:30609896).
CC {ECO:0000269|PubMed:30609896}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30609896}.
CC -!- SIMILARITY: Belongs to the Diels-Alderase family. {ECO:0000305}.
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; MK359105; AZZ09608.1; -; Genomic_DNA.
DR EMBL; MK376933; AZZ09615.1; -; Genomic_DNA.
DR SMR; A0A3Q9U4G3; -.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Isomerase.
FT CHAIN 1..371
FT /note="Diels-Alderase pvhB"
FT /id="PRO_0000453341"
SQ SEQUENCE 371 AA; 40854 MW; B004FEA3124EA2A8 CRC64;
MGNKMTKRIS HFNIENAIIP GEVSASAHVP GENNIFPKYS SNINDRTWEI WCCEGINHEG
AGVMFGFQRA AFNKKMGGGW RVQIIAVWPD GKNWYKALAL PESIFEESMA SGDITSVWKT
ADNSTNVSFT YHKVDNKIDV VVCIPGVATG KASFQGQPGD SGLSTSPSLG PYVSYMRPVG
RADMTSDMIF HFPDDGTTRQ ISFSDGHGGF DRYWGEKLWL SIQSESYFMR AFLGPYVIQI
IRLVSTEELG KQQWPIARLF HQGKLVCAPQ RCGSPDEQGI SQDTLVMSKV HDSDTGALSA
EFHDKSTGYD LTFVEAGNAR RRWTFTVRHQ TKIWSLPIGP KGGNSGFVEH VCGGLAGETC
EGLGVSGQIV Y