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VRTJ_PENAE
ID   VRTJ_PENAE              Reviewed;         388 AA.
AC   D7PHZ0;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Aldolase vrtJ {ECO:0000303|PubMed:20534346};
DE            EC=4.1.2.- {ECO:0000305|PubMed:20534346};
DE   AltName: Full=Viridicatumtoxin synthesis protein J {ECO:0000303|PubMed:20534346};
GN   Name=vrtJ {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.
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: Aldolase; part of the gene cluster that mediates the
CC       biosynthesis of viridicatumtoxin, a tetracycline-like fungal
CC       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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:O07051};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:20534346}.
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 threonine aldolase family. {ECO:0000305}.
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DR   EMBL; GU574477; ADI24936.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7PHZ0; -.
DR   SMR; D7PHZ0; -.
DR   PRIDE; D7PHZ0; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097:SF9; PTHR48097:SF9; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..388
FT                   /note="Aldolase vrtJ"
FT                   /id="PRO_0000436820"
FT   MOD_RES         241
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:O07051"
SQ   SEQUENCE   388 AA;  41800 MW;  B51C3DEE4C260362 CRC64;
     MTNSPIADLV HHPERVQSPS LVNSKMNGDA KAVTEWTEPG PAAFDFRSDT VTRPTEQMLA
     AIAATTLQDD DFRQDPTTLG LEAWMAELTG KAAGLFVVSG TMGNQLGVRA HLQSPPHSVL
     CDARSHLVTH EAGGVASLSG AMVSCVTPVN GRYMTQADLE AHVNRGTLIT DCPTRLVVLE
     IPLGGVILPL DKCRRISEWA RAQGIALHLD GARLWEAVAA GAGSLRDYCA CFDSVSLCFS
     KGLGAPIGSV LVGSETLRER ARWIRKSIGG GMRQAGVVCA AARVAVEATF LGGLLKRSHA
     RARDIATFWE IHGGRLTYPT ETNMVWLDLE AVGWTPERLI RRGAELGLRF MGARLVVHYQ
     IGDEAIGRLQ DLMLEILVSG LVDHPRDS
 
 
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