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BTCB_COLOR
ID   BTCB_COLOR              Reviewed;         534 AA.
AC   A0A484FXR4; N4VA96;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 2.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Cytochrome P450 monooxygenase btcB {ECO:0000303|Ref.3};
DE            EC=1.-.-.- {ECO:0000269|Ref.3};
DE   AltName: Full=Betaestacins biosynthesis cluster protein B {ECO:0000303|Ref.3};
GN   Name=btcB {ECO:0000303|Ref.3}; ORFNames=Cob_11438, Cob_v004821;
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=ENH79270.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=TDZ21877.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; KB726025; ENH79270.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AMCV02000011; TDZ21877.1; ALT_SEQ; Genomic_DNA.
DR   SMR; A0A484FXR4; -.
DR   EnsemblFungi; ENH79270; ENH79270; Cob_11438.
DR   eggNOG; KOG0158; Eukaryota.
DR   HOGENOM; CLU_334631_0_0_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; 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.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..534
FT                   /note="Cytochrome P450 monooxygenase btcB"
FT                   /id="PRO_0000453711"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         484
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        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   534 AA;  59697 MW;  59122DA175FE0660 CRC64;
     MASSSIASFA PFESYSPPLN TSETSLISVQ LTQDGLDYHG ALAFLCGALL FGFVYSVFYN
     LYLSPIARVP GPLIAQVSPL WLMRAVCRKQ LNCDIKKLHE KYGKKPERSP VVRLSPTEVS
     FATVEAQNAI HRPGASAKQG LFFTKEGTLE AMMGEIIWPA TNLLTATVPE EHQRLKKALQ
     PAFTEKALQL QEPIQQQHTD RLIRSVQEAS RQNRVVDLTP HMSQAIWDII SDLSFGEPLL
     KDQLAKFERL KTTFCMVSPL LEALQVLLAV PGAQTLAKAC VGLVPLLFWL PTNVLPSAQL
     RKRFERQDSN EDFLTAIMRC REMGIQMTDM ELQSNASLLV MVGYDTTATS LSATMNLLLR
     HPLCLQALQD ELHSHFSSTS DMTSKPLSQL PILNGCIQES LRLFPPANGK GTNRTSPGTM
     IDGVYIPRGV NVSADMYTIQ RSPTYWSRPN EFCPDRWFDN GPGTEFAQDV RSSHNPFLLG
     PRMCIGRAVA LQSMRMLIAK LVYTFDLEAV EDYSWDLHVA NSYLWTGYRC NARV
 
 
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