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VRTK_PENAE
ID   VRTK_PENAE              Reviewed;         534 AA.
AC   D7PHY9;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Cytochrome P450 monooxygenase vrtK {ECO:0000303|PubMed:20534346};
DE            EC=1.-.-.- {ECO:0000269|PubMed:24161266};
DE   AltName: Full=Viridicatumtoxin synthesis protein K {ECO:0000303|PubMed:20534346};
GN   Name=vrtK {ECO:0000303|PubMed:20534346};
OS   Penicillium aethiopicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=IBT 5753;
RX   PubMed=20534346; DOI=10.1016/j.chembiol.2010.03.015;
RA   Chooi Y.H., Cacho R., Tang Y.;
RT   "Identification of the viridicatumtoxin and griseofulvin gene clusters from
RT   Penicillium aethiopicum.";
RL   Chem. Biol. 17:483-494(2010).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=19168978; DOI=10.1038/ja.2008.84;
RA   Zheng C.J., Yu H.E., Kim E.H., Kim W.G.;
RT   "Viridicatumtoxin B, a new anti-MRSA agent from Penicillium sp. FR11.";
RL   J. Antibiot. 61:633-637(2008).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX   PubMed=24161266; DOI=10.1021/ja408966t;
RA   Chooi Y.H., Hong Y.J., Cacho R.A., Tantillo D.J., Tang Y.;
RT   "A cytochrome P450 serves as an unexpected terpene cyclase during fungal
RT   meroterpenoid biosynthesis.";
RL   J. Am. Chem. Soc. 135:16805-16808(2013).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=27049441; DOI=10.1038/ja.2016.35;
RA   Inokoshi J., Nakamura Y., Komada S., Komatsu K., Umeyama H., Tomoda H.;
RT   "Inhibition of bacterial undecaprenyl pyrophosphate synthase by small
RT   fungal molecules.";
RL   J. Antibiot. 69:798-805(2016).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of viridicatumtoxin, a tetracycline-like
CC       fungal meroterpenoid with a unique, fused spirobicyclic ring system
CC       (PubMed:20534346). The first step of the pathway is the production of
CC       the malonamoyl-CoA starter unit for the polyketide synthase vrtA
CC       (PubMed:20534346). The aldolase vrtJ may be involved in the synthesis
CC       of the malonamate substrate for malonamoyl-CoA synthetase vrtB
CC       (PubMed:20534346). The polyketide synthase vrtA then may utilize the
CC       malonamoyl-CoA starter unit, followed by sequential condensation of
CC       eight malonyl-CoA units to form the polyketide backbone
CC       (PubMed:20534346). The cyclization of the last ring could be mediated
CC       by the lactamase-like protein vrtG (PubMed:20534346). The proposed
CC       post-PKS tailoring steps are an hydroxylation at C5 catalyzed the
CC       cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed
CC       by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase
CC       vrtF (PubMed:20534346, PubMed:24161266). VrtC is then proposed to
CC       catalyze the transfer of a geranyl group synthesized by vrtD to the
CC       aromatic C ring of the tetracyclic polyketide intermediate of
CC       viridicatumtoxin to yield previridicatumtoxin (PubMed:20534346).
CC       Finally, the cytochrome P450 monooxygenase vrtK catalyzes the
CC       spirocyclization of the geranyl moiety of previridicatumtoxin to afford
CC       viridicatumtoxin (PubMed:24161266). {ECO:0000269|PubMed:20534346,
CC       ECO:0000269|PubMed:24161266}.
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|PubMed:20534346}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of viridicatumtoxin, but
CC       accumulates previridicatumtoxin (PubMed:24161266).
CC       {ECO:0000269|PubMed:24161266}.
CC   -!- BIOTECHNOLOGY: Viridicatumtoxin and its derivative, viridicatumtoxin B,
CC       exhibit anti-methicillin-resistant Staphylococcus aureus (anti-MRSA)
CC       activity (PubMed:19168978). Moreover, viridicatumtoxin and a C2 acetyl
CC       analog, spirohexaline, have been demonstrated to inhibit bacterial
CC       undecaprenyl diphosphate synthase, a potential new target for
CC       antibiotic development (PubMed:27049441). {ECO:0000269|PubMed:19168978,
CC       ECO:0000269|PubMed:27049441}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; GU574477; ADI24937.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7PHY9; -.
DR   SMR; D7PHY9; -.
DR   UniPathway; UPA00213; -.
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   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..534
FT                   /note="Cytochrome P450 monooxygenase vrtK"
FT                   /id="PRO_0000436826"
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"
SQ   SEQUENCE   534 AA;  60163 MW;  9E0889AF006CE344 CRC64;
     MAFSTYLGSL ESSLVLKGLA GVWLVWYIGR VFYNIFLHPL ANVPGPLLCK FSKIPWDYWQ
     WTGRLPQNTA KVHAKYGEIV RIGPNELSFT NNAAWNDIFA KVPGRAQWPR HPKRVPQGKN
     GPQSIMNTAG TYHARFRRLL NHAFSEKGLQ EQQDLITKYI DIFVSKVDGF ARTGQSLDVT
     KWFVMVGFDV ISDLGWSEPF NCVENGEVHE WMKTFAETAF DTQLKFLFRE RGLMFLAPYL
     VPMKLQLARL NNFKYARARV EERIKTGGTR GDFWDKISVK SAGDNASGEG LTKEEMVVAA
     VTLVGTGSHT ISTLLTGLAY FLGTNPHTMK KLVDEIRTSF NSPEEIDLVS VHKLKYLTAC
     LNETMRLYPP VINMLWRTPP QGGGHASGIF IPEGTGCNMS FFGIAQNPDY FTRPLDFCPE
     RFLPDPPAEF RDDNHEAYHP FSLGAYNCLG QNLANAESRL IMTKLLWYFD FELDGTVDKD
     WLDQKSYGVF IKKELPVKFH PGPNAVRHVA NGNGVATNGH ANGHANGHAR INTK
 
 
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