ADRJ_PENRW
ID ADRJ_PENRW Reviewed; 497 AA.
AC B6HV38;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Acetyltransferase adrJ {ECO:0000303|Ref.2};
DE EC=2.3.1.- {ECO:0000269|Ref.2};
DE AltName: Full=Andrastin A biosynthesis cluster protein J {ECO:0000303|Ref.2};
GN Name=adrJ {ECO:0000303|Ref.2}; ORFNames=Pc22g22910;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX DOI=10.1016/j.tet.2013.07.029;
RA Matsuda Y., Awakawa T., Abe I.;
RT "Reconstituted biosynthesis of fungal meroterpenoid andrastin A.";
RL Tetrahedron 69:8199-8204(2013).
CC -!- FUNCTION: Acetyltransferase; part of the gene cluster that mediates the
CC biosynthesis of andrastins, meroterpenoid compounds that exhibit
CC inhibitory activity against ras farnesyltransferase, suggesting that
CC they could be promising leads for antitumor agents (Ref.2). The first
CC step of the pathway is the synthesis of 3,5-dimethylorsellinic acid
CC (DMOA) by the polyketide synthase adrD via condensation of one acetyl-
CC CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2).
CC DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG
CC (Ref.2). The methyltransferase adrK catalyzes the methylation of the
CC carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is
CC further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-
CC dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then
CC catalyzes the carbon skeletal rearrangement to generate the andrastin
CC E, the first compound in the pathway having the andrastin scaffold,
CC with the tetracyclic ring system (Ref.2). The post-cyclization
CC tailoring enzymes adrF, adrE, adrJ, and adrA, are involved in the
CC conversion of andrastin E into andrastin A. The short chain
CC dehydrogenase adrF is responsible for the oxidation of the C-3 a
CC hydroxyl group of andrastin E to yield the corresponding ketone,
CC andrastin D. The ketoreductase adrE stereoselectively reduces the
CC carbonyl moiety to reverse the stereochemistry of the C-3 position to
CC yield andrastin F. The acetyltransferase adrJ is the acetyltransferase
CC that attaches the acetyl group to the C-3 hydroxyl group of andrastin F
CC to yield andrastin C. Finally, the cytochrome P450 monooxygenase adrA
CC catalyzes two sequential oxidation reactions of the C-23 methyl group,
CC to generate the corresponding alcohol andrastin B, and aldehyde
CC andrastin A (Ref.2). {ECO:0000269|Ref.2}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q70PR7}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AM920437; CAP99579.1; -; Genomic_DNA.
DR RefSeq; XP_002566185.1; XM_002566139.1.
DR AlphaFoldDB; B6HV38; -.
DR SMR; B6HV38; -.
DR EnsemblFungi; CAP99579; CAP99579; PCH_Pc22g22910.
DR GeneID; 8309017; -.
DR KEGG; pcs:Pc22g22910; -.
DR VEuPathDB; FungiDB:PCH_Pc22g22910; -.
DR eggNOG; ENOG502S6KB; Eukaryota.
DR HOGENOM; CLU_029797_2_1_1; -.
DR OMA; NTYCCRS; -.
DR OrthoDB; 643224at2759; -.
DR BioCyc; PCHR:PC22G22910-MON; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000724; Contig Pc00c22.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..497
FT /note="Acetyltransferase adrJ"
FT /id="PRO_0000446496"
FT REGION 430..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ SEQUENCE 497 AA; 55830 MW; 5748FBDB1FC3AEA9 CRC64;
MGLFSSTQPP QPTTVPSDEI IPLHFWNTAL CMRGTVLDVS LKFDDVLDVS KLRDALNRLL
EMEDWRQLGA RLRMNVDGKL EYHIPAHFDA SRPAFSMTNA QHETSIADHP LGARIPHTTG
TPAIFPSPDE LSPLLRSADA PKHIDDWTYS DRPQLCIHVI TFSDATVITI TWLHTLADVM
GMTTILNAWT ALLQGNREAI PKLQGFRSDP LTQLGQRTPA EKYMHFNRVF GRKEFLWFIG
LNIFDRLWYR QEERRTICIP ATCLRSLRQQ ASSEISATSS SEGGTVPFVS ESDVLLGWWV
RSLYGALGLR TDQTILVNNA LNLRTSLHES FMSKDSAYMG NALCMSPTFL QGQQIADEPL
GQIALRIRES VAEQRTPEQV EAMTALQMQT MEKTGYLALV GDPRMMLLSC SNWHKARLFD
MDFSPAVLQS SAQSSSQNTQ KKGKPSYVNG VQHSENSFRN VLSVIGKDAG RNWWLTGVLR
TDAWAHVEEQ VHKLGSS
