OLCL_PENCN
ID OLCL_PENCN Reviewed; 579 AA.
AC P9WEP4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=MFS-type transporter olcL {ECO:0000303|PubMed:30090271};
DE AltName: Full=15-deoxyoxalicine B biosynthesis cluster protein L {ECO:0000303|PubMed:30090271};
GN Name=olcL {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, SUBCELLULAR LOCATION, 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: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of 15-deoxyoxalicine B (PubMed:30090271). The first
CC step of the pathway is the synthesis of nicotinyl-CoA from nicotinic
CC acid by the nicotinic acid-CoA ligase olcI (PubMed:30090271).
CC Nicotinyl-CoA is then a substrate of polyketide synthase olcA to
CC produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is
CC further prenylated by the polyprenyl transferase olcH to yield
CC geranylgeranyl-HPPO (PubMed:30090271). Geranylgeranyl pyrophosphate is
CC provided by the cluster-specific geranylgeranyl pyrophosphate synthase
CC olcC (PubMed:30090271). The FAD-dependent monooxygenase olcE catalyzes
CC the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD
CC catalyzes the cyclization of the terpenoid component, resulting in the
CC formation of the tricyclic terpene moiety seen in predecaturin E
CC (PubMed:30090271). The cytochrome P450 monooxygenase then catalyzes the
CC allylic oxidation of predecaturin E, which is followed by
CC spirocylization with concomitant loss of one molecule of water to form
CC decaturin E (PubMed:30090271). Decaturin E is the substrate of the
CC cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29
CC position to form decaturin F (PubMed:30090271). The short-chain
CC dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F
CC to generate the 29-hydroxyl-27-one intermediate, and subsequent
CC hemiacetal formation probably leads to the formation of decaturin C
CC (Probable). The dioxygenase olcK may be a peroxisomal enzyme that
CC catalyzes the hydroxylation of decaturin C into decaturin A once
CC decaturin C is shuttled into the peroxisome by the MFS transporter olcL
CC (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes
CC 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 -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000305|PubMed:30090271}; Multi-pass membrane protein
CC {ECO:0000255}. Note=OlcL may be inserted in the peroxisomal membrane
CC viathe import receptor pex19. {ECO:0000305|PubMed:30090271}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of 15-deoxyoxalicine B
CC and accumulates decaturin C and 5-deoxyoxalicine A.
CC {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 major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR SMR; P9WEP4; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Peroxisome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..579
FT /note="MFS-type transporter olcL"
FT /id="PRO_0000453896"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 579 AA; 62278 MW; 8A8CAA30E87A5691 CRC64;
MANIGGSNAV SSAQGSQISD SPTTVDDRLD EHKETSTQSI DHSENITQSP TSLQKPPDES
NATPVGFGED GCQSDSQEYP NSWRLAAIMI GVCLAVFSMA LDNTILATAI PKITDQFTSL
GDVGWYGSVY PLTNCCLTLV FGKLYTFYST KWVYLSALAV FEIGSLICGA TPSSLGLIIG
RAIAGLGSSG IYLGSMIILS QSVPLQKRPL FTSLVGGLYG VAGVAGPLLG GAFTDYVSWR
WCFYINPLFG AVTALFILLF FDGKEPIKSP GKIKEQISQF DLIGLFFFLP GMISLLLALQ
WGGQQYNWQS GRIIGLFVCS ICLLSIFIMV QWRQKEKATV TLRMIKNKNV WGASLFNFCI
TGSFLVFSYY LPVWFQSIKN VSATKSGLMN LPMLLGVILC SIISGYGVGR IGYYTPFMYA
APIVSAIGAG LLSTFQANFG PSQWIGYQAL YGIGLGLGLS QPIVVIQAAI PLIDIPSAIA
IVTFIQSLGG SVSVSIAQNV FRNELLRGLA QNAPKVDAHK LITAGPTTLR YVVPAELLER
VLVAYNSAIT HAFYVGAAFS VLAMIGALPI QWISVKGRE
