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
