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BRAD_ANNTR
ID   BRAD_ANNTR              Reviewed;         245 AA.
AC   P9WER3; A0A866WLG1;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   23-FEB-2022, entry version 2.
DE   RecName: Full=Brasilane terpene glycosides biosynthesis cluster protein D {ECO:0000303|PubMed:32936132};
GN   Name=braD {ECO:0000303|PubMed:32936132};
OS   Annulohypoxylon truncatum (Hypoxylon truncatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Annulohypoxylon.
OX   NCBI_TaxID=327061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=DSM 103480 / CBS 140778;
RX   PubMed=32936132; DOI=10.1039/d0cc03950k;
RA   Feng J., Surup F., Hauser M., Miller A., Wennrich J.P., Stadler M.,
RA   Cox R.J., Kuhnert E.;
RT   "Biosynthesis of oxygenated brasilane terpene glycosides involves a
RT   promiscuous N-acetylglucosamine transferase.";
RL   Chem. Commun. (Camb.) 56:12419-12422(2020).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       the brasilane terpene glycosides brasilane D and E (PubMed:32936132).
CC       The biosynthesis starts with the activity of the terpene cyclase braA
CC       that converts farnesyl pyrophosphate into the sesquiterpene alcohol
CC       trichobrasilenol (PubMed:32936132). Subsequently, trichobrasilenol is
CC       glycosylated by the O-glycosyltransferase braB putatively using UDP-
CC       GlcNAc as sugar donor to yield brasilane A (PubMed:32936132). The
CC       latter then undergoes two rounds of oxidation performed by the
CC       cytochrome P450 monooxygenase braC (PubMed:32936132). In the first
CC       round braC hydroxylates C-12 forming brasilane D, which serves as
CC       substrate in the second round to establish the epoxide at the bond
CC       between C-5 and C-10 and oxidize the alcohol at C-12 to an aldehyde
CC       leading to the final product brasilane E (PubMed:32936132).
CC       {ECO:0000269|PubMed:32936132}.
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DR   EMBL; MT383109; QOE88886.1; -; Genomic_DNA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   4: Predicted;
KW   Metal-binding; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..245
FT                   /note="Brasilane terpene glycosides biosynthesis cluster
FT                   protein D"
FT                   /id="PRO_0000453909"
FT   ZN_FING         121..152
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         161..185
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          186..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   245 AA;  26631 MW;  524BC59DB0EEAD21 CRC64;
     MSSDLVSKGM AQVFTGLGIL LGAGRISSET HEEIMALLSA DPGSNTGIMT GTNTGSTSII
     PTQSKRVDMG DIPAGLPRPG KETPVSIQSH DLLGLGADLS TEAVQPPETF RAQASPSAPS
     KELKIICPWW LTDGYSCREH DQGKCPFYHD NVAGGVKHPL ICHFWADGGR CTKSQKDCRF
     AHYPAPHRVT APMPSKKKSK KLRSSVADDA SHPDLGKARR HDPRDDEQND EVWRNQGRAR
     PGQEW
 
 
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