TPCC_COCH5
ID TPCC_COCH5 Reviewed; 525 AA.
AC M2UJ60;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Cytochrome P450 monooxygenase tpcC {ECO:0000303|PubMed:29417814};
DE EC=1.-.-.- {ECO:0000269|PubMed:29417814};
DE AltName: Full=Terpestacin biosynthesis cluster protein C {ECO:0000303|PubMed:29417814};
GN Name=tpcC {ECO:0000303|PubMed:29417814}; ORFNames=COCHEDRAFT_1212392;
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O;
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O;
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
RN [3]
RP FUNCTION.
RX PubMed=29185768; DOI=10.1021/acs.orglett.7b03418;
RA Narita K., Sato H., Minami A., Kudo K., Gao L., Liu C., Ozaki T.,
RA Kodama M., Lei X., Taniguchi T., Monde K., Yamazaki M., Uchiyama M.,
RA Oikawa H.;
RT "Focused genome mining of structurally related sesterterpenes: enzymatic
RT formation of enantiomeric and diastereomeric products.";
RL Org. Lett. 19:6696-6699(2017).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=29417814; DOI=10.1021/acs.joc.7b03220;
RA Narita K., Minami A., Ozaki T., Liu C., Kodama M., Oikawa H.;
RT "Total biosynthesis of antiangiogenic agent (-)-terpestacin by artificial
RT reconstitution of the biosynthetic machinery in Aspergillus oryzae.";
RL J. Org. Chem. 83:7042-7048(2018).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of terpestacin (PubMed:29185768). The
CC bifunctional terpene synthase tpcA converts isopentenyl diphosphate
CC (IPP) and dimethylallyl diphosphate (DMAPP) into the sesterterpene
CC preterpestacin I (PubMed:29185768). The C-terminal prenyltransferase
CC (PT) domain of tpcA catalyzes formation of GFPP, whereas the N-terminal
CC terpene cyclase (TC) domain catalyzes the cyclization of GFPP into
CC preterpestacin I (PubMed:29185768). The cytochrome P450 monooxygenase
CC tpcB then hydroxylates preterpestacin I to yield 24-
CC hydroxypreterpstacin I (renamed as preterpestacin II) whereas the
CC cytochrome P450 monooxygenase tpcC further hydroxylates preterpestacin
CC II to yield 16,17-dihydroxypreterpestacin II (renamed as preterpestacin
CC III) (PubMed:29417814). Finally, the FAD-dependent monooxygenase tpcD
CC converts preterpestacin III into terpestacin (PubMed:29417814).
CC {ECO:0000269|PubMed:29185768, ECO:0000269|PubMed:29417814}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:29417814}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KB445573; EMD93706.1; -; Genomic_DNA.
DR SMR; M2UJ60; -.
DR EnsemblFungi; EMD93706; EMD93706; COCHEDRAFT_1212392.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_4_1; -.
DR OMA; VMPEDSK; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000016936; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..525
FT /note="Cytochrome P450 monooxygenase tpcC"
FT /id="PRO_0000453716"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 457
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 525 AA; 59551 MW; CF77B69DF691CDBF CRC64;
MAILSSALVT IDLPVTLVSL LVGSIFYFCY LTVYRLFLSP IAHFPGPKLA AWTYWYEFWY
DVIAEPEYTF KIGRLHKIYG PVVRINPDEI HIADPDFYDT IYAGSGRKRD KWDWITRSFG
VDESLIGTLK HDEHRVRRAS LSPYFSKQSV RALQPLIDRN MAILLDRLRE FAKSGSPLKL
DDAYAALTND IVEDYAFGRS DHRLEAPDFD PSFRDAMLQG GKAGHVLKHF TWLMDLLKKL
PDSLLLKLSP AMGAYSQLQT SVKRQVAEIQ HAHQMHTYDK TRRTIFHEIL NSKLSDYDKS
TDRLWQEGEV VVAAGTITTA WALGVSTYFV LATPDILRKL KTELEAAIPD PSQPLNLITL
EALPFLTGVV QEGVRLSHAI SHRLHRICPD ETLIYQDNDN QREWRIPPGT PLSMTSNLVH
HDERVFPDSH AFKPERWLDN ARLERYLVSF GKGGRACLGI NLAYAELYLT LAALFRVYGT
EQVKGKDDVG TLQLFETSAA DLVITSDTVV PVMPEDSKGL RVKVS
