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MACE_PENTR
ID   MACE_PENTR              Reviewed;         260 AA.
AC   A0A2P1DP82;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=Oxidoreductase macE {ECO:0000303|PubMed:28926261};
DE            EC=1.-.-.- {ECO:0000250|UniProtKB:G3Y423};
DE   AltName: Full=Macrophorins biosynthesis cluster protein E {ECO:0000303|PubMed:28926261};
GN   Name=macE {ECO:0000303|PubMed:28926261};
OS   Penicillium terrestre.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=374132;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=LM2;
RX   PubMed=28926261; DOI=10.1021/acs.orglett.7b02653;
RA   Tang M.C., Cui X., He X., Ding Z., Zhu T., Tang Y., Li D.;
RT   "Late-stage terpene cyclization by an integral membrane cyclase in the
RT   biosynthesis of isoprenoid epoxycyclohexenone natural products.";
RL   Org. Lett. 19:5376-5379(2017).
CC   -!- FUNCTION: Oxidoreductase; part of the gene cluster that mediates the
CC       biosynthesis of macrophorins, isoprenoid epoxycyclohexenones containing
CC       cyclized drimane moieties (PubMed:28926261). The first step of the
CC       pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the
CC       polyketide synthase macA (PubMed:28926261). 6-MSA is then converted to
CC       m-cresol by the decarboxylase macB (By similarity). The cytochrome P450
CC       monooxygenase macC then catalyzes the oxidation of m-cresol to
CC       toluquinol (By similarity). Epoxidation of toluquinol is then performed
CC       by the short chain dehydrogenase macD, with the help of macE, and a
CC       further prenylation by macG leads to 7-deacetoxyyanuthone A (By
CC       similarity). The next step is the hydroxylation of C-22 of 7-
CC       deacetoxyyanuthone A by the cytochrome P450 monooxygenase macH to yield
CC       22-deacetylyanuthone A (By similarity). O-Mevalon transferase macI then
CC       attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to
CC       produce yanuthone E (By similarity). The terpene cyclase macJ catalyzes
CC       the cyclization of 22-deacetylyanuthone A to macrophorin A
CC       (PubMed:28926261). MacJ is also able to catalyze cyclization of
CC       yanuthone E and 7-deacetoxyyanuthone A to their corresponding
CC       macrophorins (PubMed:28926261). The macJ products can be further
CC       modified by macH and macJ, as well as by the FAD-dependent
CC       monooxygenase macF, to produce additional macrophorins, including 4'-
CC       oxomacrophorin A, 4'-oxomacrophorin D and 4'-oxomacrophorin E
CC       (PubMed:28926261). {ECO:0000250|UniProtKB:G3Y423,
CC       ECO:0000269|PubMed:28926261}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:28926261}.
CC   -!- MISCELLANEOUS: The macrophorins cluster contains a single gene
CC       insertion (encoding for the terpene cyclase macJ) compared with the
CC       yanuthone cluster that produces the linear compound yanuthone.
CC       {ECO:0000269|PubMed:28926261}.
CC   -!- SIMILARITY: Belongs to the oxidoreductase OpS7 family. {ECO:0000305}.
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DR   EMBL; MF990003; AVK70104.1; -; Genomic_DNA.
DR   EMBL; MH388470; QBC75444.1; -; Genomic_DNA.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..260
FT                   /note="Oxidoreductase macE"
FT                   /id="PRO_0000454089"
SQ   SEQUENCE   260 AA;  29586 MW;  5AB3A043B86020D4 CRC64;
     MAPCKPRTFT AGQDPLTKFD GAISVRNLPR PPDRLFLFHG IMRPSRGIYA KLIATGQKPP
     THFHPSQWEF FRVLRGNLTI DFNGRAIHRT ASDGELAVPP YTHHVIYGTP GTEMNEVEFV
     VSASDPAAEE QGATVMDQPF FENWYGYQED VFQRGEKLDF IQVLSMFDAG GTYLSPPWWV
     PFRSWVGLFL GIVVGRWIGG LLGYAPFYPE WTTDWEAACE TMQQSWFQRR FADPQAQERA
     REKFRGQLEQ EASAKGGKSE
 
 
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