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P4501_NEOBT
ID   P4501_NEOBT             Reviewed;         486 AA.
AC   Q6F5E4;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Cytochrome P450 monooxygenase 1 {ECO:0000303|PubMed:14745177};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21897020};
DE   AltName: Full=Aphidicolin biosynthesis protein PbP450-1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PbP450-1;
OS   Neocamarosporium betae (Beet black rot fungus) (Pleospora betae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Neocamarosporium.
OX   NCBI_TaxID=1979465;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION OF GENE CLUSTER.
RC   STRAIN=PS-16;
RX   PubMed=14745177; DOI=10.1271/bbb.68.146;
RA   Toyomasu T., Nakaminami K., Toshima H., Mie T., Watanabe K., Ito H.,
RA   Matsui H., Mitsuhashi W., Sassa T., Oikawa H.;
RT   "Cloning of a gene cluster responsible for the biosynthesis of diterpene
RT   aphidicolin, a specific inhibitor of DNA polymerase alpha.";
RL   Biosci. Biotechnol. Biochem. 68:146-152(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=11457369; DOI=10.1021/ja015747j;
RA   Oikawa H., Toyomasu T., Toshima H., Ohashi S., Kawaide H., Kamiya Y.,
RA   Ohtsuka M., Shinoda S., Mitsuhashi W., Sassa T.;
RT   "Cloning and functional expression of cDNA encoding aphidicolan-16 beta-ol
RT   synthase: a key enzyme responsible for formation of an unusual diterpene
RT   skeleton in biosynthesis of aphidicolin.";
RL   J. Am. Chem. Soc. 123:5154-5155(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=21897020; DOI=10.1271/bbb.110366;
RA   Fujii R., Minami A., Tsukagoshi T., Sato N., Sahara T., Ohgiya S., Gomi K.,
RA   Oikawa H.;
RT   "Total biosynthesis of diterpene aphidicolin, a specific inhibitor of DNA
RT   polymerase alpha: heterologous expression of four biosynthetic genes in
RT   Aspergillus oryzae.";
RL   Biosci. Biotechnol. Biochem. 75:1813-1817(2011).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of aphidicolin, a specific inhibitor of
CC       eukaryotic DNA synthesis and DNA polymerase alpha (PubMed:14745177,
CC       PubMed:21897020). The geranylgeranyl pyrophosphate synthase GGS is
CC       required for supplying a sufficient amount of geranylgeranyl
CC       diphosphate (GGDP), the general precursor of diterpenes
CC       (PubMed:21897020). The diterpene synthase ACS then catalyzes the
CC       conversion of geranylgeranyl diphosphate to aphidicolan-16-beta-ol via
CC       the intermediate syn-copalyldiphosphate (syn-CDP) (PubMed:11457369,
CC       PubMed:21897020). In addition to aphidicolan-16-beta-ol, the enzyme
CC       produces also low levels of amphidicol-15-ene and amphidicol-16-ene
CC       (PubMed:11457369). The cytochrome P450 monooxygenase P450-2 then
CC       catalyzes the two-step hydroxylation from aphidicolan-16-beta-ol to 3-
CC       deoxyaphidicolin via a 17,3-deoxyaphidicolin intermediate
CC       (PubMed:21897020). Finally, the cytochrome P450 monooxygenase P450-1
CC       converts 3-deoxyaphidicolin to aphidicolin (PubMed:21897020).
CC       {ECO:0000269|PubMed:11457369, ECO:0000269|PubMed:14745177,
CC       ECO:0000269|PubMed:21897020}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:21897020}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB079898; BAD29966.1; -; mRNA.
DR   EMBL; AB114137; BAD29972.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6F5E4; -.
DR   SMR; Q6F5E4; -.
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   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; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..486
FT                   /note="Cytochrome P450 monooxygenase 1"
FT                   /id="PRO_0000438555"
FT   BINDING         430
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        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   486 AA;  54911 MW;  BE0158FEB3ED5B95 CRC64;
     MSHFLPTLIL TSLTLVAYVL ARMIYNVFYH PLSAFPGDAF FCATGLTKAY HMIAGDLQLK
     VKDMHDKYGS VVRIAPTELS FSYCSAWKDI YGSRGGRELS KFYDFYRVDE AMPQHIISAG
     KAKHSILRRY LAHGFSENAM KAQEPVILDL VNLLMQRLRE HAEEGARVVD VNKWFNFATF
     EIIGKLTFGA DLGNLRNRDW HPWVKGSANN NMVVGFMAAA NSVGLGPIIK WCISNEILPR
     QKYLDELAEM VQKRTGVTVE RPDFIQGLLR DDVQLSNGEI VANVEALIGA GSESTATLLT
     GTVCALLQNP DQLAKVIDEV RSTFRTEDEI TLHSVQRLDY MLACLNETFR YYPPVTNGMP
     RVTPKEGAII GGRLVPGNTV VAIWQWAICH DPALWKDPYT FRPERFLEAP EFSTDVREAL
     NPFSVGTRNC IGRNLSYAET RLILARLFYY FDLELADPDQ DWFGAQKAYL VWDAPALNMY
     LKPVVR
 
 
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