BTCC_COLOR
ID BTCC_COLOR Reviewed; 520 AA.
AC A0A484FVL2; N4UU25;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Cytochrome P450 monooxygenase btcC {ECO:0000303|Ref.3};
DE EC=1.-.-.- {ECO:0000269|Ref.3};
DE AltName: Full=Betaestacins biosynthesis cluster protein C {ECO:0000303|Ref.3};
GN Name=btcC {ECO:0000303|Ref.3}; ORFNames=Cob_11436, Cob_v004819;
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=30893003; DOI=10.1094/mpmi-12-18-0352-a;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX DOI=10.1016/j.tetlet.2018.02.022;
RA Gao L., Narita K., Ozaki T., Kamukara N., Gan P., Minami A., Liu C.,
RA Lei X., Shirasu K., Oikawa H.;
RT "Identification of novel sesterterpenes by genome mining of phytopathogenic
RT fungi Phoma and Colletotrichum sp.";
RL Tetrahedron Lett. 59:1136-1139(2018).
CC -!- FUNCTION: Cytochrome P4590 monooxygenase part of the gene cluster that
CC mediates the biosynthesis of betaestacins (Ref.3). The bifunctional
CC terpene synthase btcA converts isopentenyl diphosphate (IPP) and
CC dimethylallyl diphosphate (DMAPP) into the sesterterpene betaestacin I
CC (Ref.3). The C-terminal prenyltransferase (PT) domain of btcA catalyzes
CC formation of GFPP, whereas the N-terminal terpene cyclase (TC) domain
CC catalyzes the cyclization of GFPP into betaestacin I (Ref.3). The
CC cytochrome P450 monooxygenase btcB oxidizes the C25 methyl group of
CC betaestacin I to yield the carboxylic acid betaestacin IV via the
CC alcohol betaestacin III (Ref.3). The cytochrome P450 monooxygenase btcC
CC further catalyzes the multistep oxidation of betaestacin IV to produce
CC several compounds, including betaestacins Va, Vb, Vc and VI (Ref.3).
CC {ECO:0000269|Ref.3}.
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|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ENH79268.1; Type=Erroneous gene model prediction; Evidence={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; KB726025; ENH79268.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AMCV02000011; TDZ22090.1; -; Genomic_DNA.
DR STRING; 5465.ENH79268; -.
DR EnsemblFungi; ENH79268; ENH79268; Cob_11436.
DR eggNOG; KOG0159; Eukaryota.
DR HOGENOM; CLU_001570_14_11_1; -.
DR OrthoDB; 467733at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000014480; 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 PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Cytochrome P450 monooxygenase btcC"
FT /id="PRO_0000453712"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 448
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"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 520 AA; 59351 MW; F93BA166B43596E8 CRC64;
MIFLLTLAGL KVLSIVILFG IIYLFASSIY NLYFHPLSRF PGPFLARAQD FWVSRQWISG
NWPWEVEALH AKYGDIVRIG PNELSCAHPQ SIKDIYGQPN INHPQFFRKF TTFYKQTDVG
GSIGTEVDPH IHQGIRKRLA PGFSVSALSK QSDIVIRHID SLLHQVSRNG QCQSGMNMSQ
WFMWLAFDVI VDLSFGEELG TVETGTGNDW INMLANSGFQ IALGYVVRRR WKALQDLVRY
CLVNEKSKSM RTKYIANARE KARQRLERGA DVERFDFFSH LLREKAPEAN IDFFASQGTT
LVAAGTETTS TFMSALTYYL LQNPRALDRL QEELRRSFKH HSEIDGESTK SLKYLNAAIE
EGMRIFAPAP FGLPRVSPGA MVSGEWIPKG SIIATAAHVT SRDERWFFKS KEFHPERWLP
LDHPHYDHIF SKDRKDASKP FSIGSRSCIG IHLSYMEVRI CVSKLAWSFD WEQVSAHEDF
VKDARLLGLW KAAPFHVRYQ PYPGAEPPVM NHSKINSDLA
