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CDMC_TALVE
ID   CDMC_TALVE              Reviewed;         417 AA.
AC   A0A3G9GUR6;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Acetyltransferase cdmC {ECO:0000303|PubMed:30417647};
DE            EC=2.3.1.- {ECO:0000305|PubMed:30417647};
DE   AltName: Full=chrodrimanin B biosynthesis cluster protein C {ECO:0000303|PubMed:30417647};
GN   Name=cdmC {ECO:0000303|PubMed:30417647};
OS   Talaromyces verruculosus (Penicillium verruculosum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=198730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=TPU1311;
RX   PubMed=30417647; DOI=10.1021/acs.orglett.8b03268;
RA   Bai T., Quan Z., Zhai R., Awakawa T., Matsuda Y., Abe I.;
RT   "Elucidation and heterologous reconstitution of chrodrimanin B
RT   biosynthesis.";
RL   Org. Lett. 20:7504-7508(2018).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=26115570; DOI=10.1016/j.bmcl.2015.06.026;
RA   Yamazaki H., Nakayama W., Takahashi O., Kirikoshi R., Izumikawa Y.,
RA   Iwasaki K., Toraiwa K., Ukai K., Rotinsulu H., Wewengkang D.S.,
RA   Sumilat D.A., Mangindaan R.E., Namikoshi M.;
RT   "Verruculides A and B, two new protein tyrosine phosphatase 1B inhibitors
RT   from an Indonesian ascidian-derived Penicillium verruculosum.";
RL   Bioorg. Med. Chem. Lett. 25:3087-3090(2015).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=25902139; DOI=10.1371/journal.pone.0122629;
RA   Xu Y., Furutani S., Ihara M., Ling Y., Yang X., Kai K., Hayashi H.,
RA   Matsuda K.;
RT   "Meroterpenoid Chrodrimanins Are Selective and Potent Blockers of Insect
RT   GABA-Gated Chloride Channels.";
RL   PLoS ONE 10:E0122629-E0122629(2015).
CC   -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of chrodrimanin B, a meroterpenoid that acts as a potent
CC       blocker of insect GABA-gated chloride channels (PubMed:30417647). The
CC       first step of the pathway is the biosynthesis of 6-hydroxymellein by
CC       the polyketide synthase cdmE (PubMed:30417647). The prenyltransferase
CC       cdmH acts as a 6-hydroxymellein 5-farnesyltransferase and produces the
CC       hydrophobic metabolite verruculide C (PubMed:30417647). The FAD-
CC       dependent monooxygenase cdmI further converts verruculide C into
CC       verruculide B (PubMed:30417647). The terpene cyclase cdmG then produced
CC       the pentacyclic molecule 3-hydroxypentacecilide A, the backbone
CC       structure of chrodrimanin B, via folding the farnesyl moiety of the
CC       substrate into the chair-boat conformation (PubMed:30417647). The
CC       short-chain dehydrogenase/reductase cdmF functions as the 3-OH
CC       dehydrogenase that oxidizes the C-3 hydroxyl group of 3-
CC       hydroxypentacecilide A and produces chrodrimanin C, the dehydrogenated
CC       product of 3-hydroxypentacecilide A (PubMed:30417647). The cytochrome
CC       P450 monooxygenase cdmJ then accepts both 3-hydroxypentacecilide A and
CC       chrodrimanin C and functions as a C-7-beta-hydroxylase to produce
CC       respectively chrodrimanin H and chrodrimanin F (PubMed:30417647). The
CC       dioxygenase cdmA accepts chrodrimanin H to afford chrodrimanin E, which
CC       is further transformed to chrodrimanin A by the dioxygenase cdmD
CC       (PubMed:30417647). CdmA can also accept chrodrimanin C as substrate to
CC       convert it into verruculide A, which is further converted into
CC       chrodrimanin T by cdmD (PubMed:30417647). The last step of the
CC       biosynthesis is proposed to be performed by the acetyltransferase cdmC
CC       which acetylates chrodrimanin A to yield chrodrimanin B (Probable). The
CC       pathway may also lead to the production of additional shunt products,
CC       including chrodrimanins T and U (PubMed:30417647).
CC       {ECO:0000269|PubMed:30417647, ECO:0000305|PubMed:30417647}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + chrodrimanin A = chrodrimanin B + CoA;
CC         Xref=Rhea:RHEA:65324, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:156418, ChEBI:CHEBI:156420;
CC         Evidence={ECO:0000269|PubMed:30417647};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65325;
CC         Evidence={ECO:0000269|PubMed:30417647};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:30417647}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: Compounds in the chrodrimanin family such as
CC       chrodrimanin A or verruculide A exhibit strong inhibitory activities
CC       against protein tyrosine phosphatase 1B (PTP1B) and therefore, they
CC       could potentially be developed into drugs for the treatment of type 2
CC       diabetes or obesity (PubMed:26115570). Furthermore, chrodrimanin B, the
CC       end product of the pathway involving chrodrimanin A or verruculide A,
CC       does not exhibit the PTP1B inhibitory activity, while it functions as a
CC       potent blocker of insect GABA-gated chloride channels
CC       (PubMed:25902139). {ECO:0000269|PubMed:25902139,
CC       ECO:0000269|PubMed:26115570}.
CC   -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR   EMBL; LC422696; BBG28482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G9GUR6; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR044851; Wax_synthase.
DR   InterPro; IPR032805; Wax_synthase_dom.
DR   PANTHER; PTHR31595; PTHR31595; 1.
DR   Pfam; PF13813; MBOAT_2; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Glycoprotein; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..417
FT                   /note="Acetyltransferase cdmC"
FT                   /id="PRO_0000449129"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   417 AA;  48180 MW;  BE2B83CF0181E98C CRC64;
     MLSLEPLSRP VLDSSQTLLV IFLLAFTRQN SIFRYLSIPV LTFIVKEQIT QPPAVVENFH
     QWLNESSVPF NYLHHINILA LTSIDLRNDN NGVLPGLFDR IKSAFIYQLN PRGVGTRYQV
     KNIPPVPEYY KKRKGYLSQR YRFVVRQLCL FVWQYLIVDV GCSLWHNLPD QERFALFGPG
     TEWNIINAGP QQWKVRLMAA MIFWTTARNA VDLSHRLGSA VLTGIGATSV HEWPPMCGSL
     RDAYTLRNLW GKWWHQQLRW TLSSHSNFVT RRLLKLPRRS LLERYLNNAI VHVFSAFIHV
     NGWRLAGIPD GYIGPSLFYM SFVGGYLVED FVQHIWATLF RSRSRTSTGI FFERLTGIFW
     VATFLTVTTP WWIYPLLRRE HSFALPVSLV ESVGMNNALA MIGVGAFILK TRFDANI
 
 
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