OLCF_PENCN
ID OLCF_PENCN Reviewed; 258 AA.
AC P9WEQ5;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=Short-chain dehydrogenase/reductase olcF {ECO:0000303|PubMed:30090271};
DE EC=1.1.1.- {ECO:0000269|PubMed:30090271};
DE AltName: Full=15-deoxyoxalicine B biosynthesis cluster protein F {ECO:0000303|PubMed:30090271};
GN Name=olcF {ECO:0000303|PubMed:30090271};
OS Penicillium canescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5083;
RN [1]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=30090271; DOI=10.1039/c5sc01965f;
RA Yaegashi J., Romsdahl J., Chiang Y.M., Wang C.C.C.;
RT "Genome mining and molecular characterization of the biosynthetic gene
RT cluster of a diterpenic meroterpenoid, 15-deoxyoxalicine B, in Penicillium
RT canescens.";
RL Chem. Sci. 6:6537-6544(2015).
RN [2]
RP ERRATUM OF PUBMED:30090271.
RX PubMed=30123464; DOI=10.1039/c6sc90012g;
RA Yaegashi J., Romsdahl J., Chiang Y.M., Wang C.C.C.;
RT "Correction: Genome mining and molecular characterization of the
RT biosynthetic gene cluster of a diterpenic meroterpenoid, 15-deoxyoxalicine
RT B, in Penicillium canescens.";
RL Chem. Sci. 7:2440-2440(2016).
CC -!- FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of 15-deoxyoxalicine B
CC (PubMed:30090271). The first step of the pathway is the synthesis of
CC nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI
CC (PubMed:30090271). Nicotinyl-CoA is then a substrate of polyketide
CC synthase olcA to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one
CC (HPPO) which is further prenylated by the polyprenyl transferase olcH
CC to yield geranylgeranyl-HPPO (PubMed:30090271). Geranylgeranyl
CC pyrophosphate is provided by the cluster-specific geranylgeranyl
CC pyrophosphate synthase olcC (PubMed:30090271). The FAD-dependent
CC monooxygenase olcE catalyzes the epoxidation of geranylgeranyl-HPPO and
CC the terpene cyclase olcD catalyzes the cyclization of the terpenoid
CC component, resulting in the formation of the tricyclic terpene moiety
CC seen in predecaturin E (PubMed:30090271). The cytochrome P450
CC monooxygenase then catalyzes the allylic oxidation of predecaturin E,
CC which is followed by spirocylization with concomitant loss of one
CC molecule of water to form decaturin E (PubMed:30090271). Decaturin E is
CC the substrate of the cytochrome P450 monooxygenase olcJ which
CC hydroxylates it at the C-29 position to form decaturin F
CC (PubMed:30090271). The short-chain dehydrogenase/reductase olcF may
CC catalyze the oxidation of decaturin F to generate the 29-hydroxyl-27-
CC one intermediate, and subsequent hemiacetal formation probably leads to
CC the formation of decaturin C (Probable). The dioxygenase olcK may be a
CC peroxisomal enzyme that catalyzes the hydroxylation of decaturin C into
CC decaturin A once decaturin C is shuttled into the peroxisome by the MFS
CC transporter olcL (Probable). Finally the cytochrome P450 monooxygenase
CC olcB catalyzes the oxidative rearrangement to yield 15-deoxyoxalicine B
CC (PubMed:30090271). In the absence of olcJ, decaturin E may be shunted
CC to a pathway in which it is oxidized to a ketone, possibly by olcF, to
CC form decaturin D, which undergoes further allylic oxidation to yield
CC decaturin G (PubMed:30090271). Moreover, in the absence of oclK or
CC oclL, oclB can convert decaturin C into 15-deoxyoxalicine A
CC (PubMed:30090271). {ECO:0000269|PubMed:30090271,
CC ECO:0000305|PubMed:30090271}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:30090271}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of 15-deoxyoxalicine B
CC and accumulates decaturin F. {ECO:0000269|PubMed:30090271}.
CC -!- MISCELLANEOUS: The 15-deoxyoxalicine B cluster is a rare cluster that
CC contains its own geranylgeranyl pyrophosphate synthase (olcC), in
CC contrast to other related clusters which rely on a FPP/GGPP synthase
CC localized outside of the cluster. {ECO:0000269|PubMed:30090271}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR SMR; P9WEQ5; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..258
FT /note="Short-chain dehydrogenase/reductase olcF"
FT /id="PRO_0000453892"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 35..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 158..162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 258 AA; 27388 MW; 42B3523C7F1391DC CRC64;
MMGVLEDQVI IVTGAASGIG MATAIAALRE GARVFGVDIA PQPATLKENN KFRYAQCDLA
VESSIDSVVS NCLEVFEGRI DALFNIAGVM DHHGSVDTVT DSDWDRCIAI NLTAPLKLMR
AVIPTMRAHK RGNIINMSSR AGVSGAAAGV AYTASKHGLI GLSKNVAWRF KGDNIRCNVV
CPGGVATGII SNMDPSQFDH EALDTIKPIL GAVYSNRPEG YTQMLPEEVA ETVIFLASDQ
SARINGAVLP VDDAWSTI
