TPCD_COCH5
ID TPCD_COCH5 Reviewed; 518 AA.
AC M2T7Z1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=FAD-dependent monooxygenase tpcD {ECO:0000303|PubMed:29417814};
DE EC=1.-.-.- {ECO:0000269|PubMed:29417814};
DE AltName: Full=Terpestacin biosynthesis cluster protein D {ECO:0000303|PubMed:29417814};
DE Flags: Precursor;
GN Name=tpcD {ECO:0000303|PubMed:29417814}; ORFNames=COCHEDRAFT_1171747;
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: FAD-dependent 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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:29185768}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; KB445573; EMD93705.1; -; Genomic_DNA.
DR SMR; M2T7Z1; -.
DR STRING; 5016.M2T7Z1; -.
DR EnsemblFungi; EMD93705; EMD93705; COCHEDRAFT_1171747.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_2_1; -.
DR OMA; CSFGWEW; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000016936; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..518
FT /note="FAD-dependent monooxygenase tpcD"
FT /id="PRO_5012542481"
FT DOMAIN 75..246
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 112
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:P08159"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 518 AA; 55674 MW; 17A92B889FF3F048 CRC64;
MQLLGTLSWL YAIQASIGSS KAVTADYGSC HDACTLLSGT LSVELGGSHV SDYKHYPTIA
NGSSVASLFW AQQQQSAQPA CLVHVYSPQD VATVISVSRS TNCPFAVRGG GHSDIPGASN
INGGITVNMA ALSNVELHES EGLARVGAGA RWGDVYKELE KSNKTVVGGR LTGVGVGGLV
LGGGLSHFSG LHGWACDNVR NYEVVLANGT LVIASNSSNP DLYRALRGGG NSFGVVTRFD
LDVFQQGPMW GGLHVWPFQP SVTSAITRGF VEFAHNAPSD PHVSLFAGLG YKQGGFAWAV
GQYDALGRVE PPIFTQFKDD VEVYGTAKIV STARLTSLSD LADELNQSEP AGIRSRFTTA
TFTADAELLI LIVEFFEEQV QKALDKGLDK DQRFAPMLGI QPLTQNLLRA QETRGGNVMG
LRDLDAPLVV CSFGWEWSYE SDDKVVIDGI KAVLDHSVSA AKEKGLYHPF KYMNYAALDQ
DPIESYGKEN IEFLKRVRAM YDPEGVFTNL VPGGHKIN
