CNSK_PENEN
ID CNSK_PENEN Reviewed; 466 AA.
AC A0A0A2JWD5;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Communesin N16 acyltransferase cnsK {ECO:0000303|PubMed:25571861};
DE EC=2.3.1.- {ECO:0000269|PubMed:25571861};
DE AltName: Full=Communesin biosynthesis cluster protein K {ECO:0000303|PubMed:25571861};
GN Name=cnsK {ECO:0000303|PubMed:25571861}; ORFNames=PEX2_055450;
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8;
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
RN [2]
RP IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=25571861; DOI=10.1002/anie.201411297;
RA Lin H.C., Chiou G., Chooi Y.H., McMahon T.C., Xu W., Garg N.K., Tang Y.;
RT "Elucidation of the concise biosynthetic pathway of the communesin indole
RT alkaloids.";
RL Angew. Chem. Int. Ed. 54:3004-3007(2015).
RN [3]
RP FUNCTION.
RX PubMed=26963294; DOI=10.1021/jacs.6b01413;
RA Lin H.C., McMahon T.C., Patel A., Corsello M., Simon A., Xu W., Zhao M.,
RA Houk K.N., Garg N.K., Tang Y.;
RT "P450-mediated coupling of indole fragments to forge communesin and
RT unnatural isomers.";
RL J. Am. Chem. Soc. 138:4002-4005(2016).
CC -!- FUNCTION: Communesin N16 acyltransferase; part of the gene cluster that
CC mediates the biosynthesis of communesins, a prominent class of indole
CC alkaloids with great potential as pharmaceuticals (PubMed:25571861).
CC Communesins are biosynthesized by the coupling of tryptamine and
CC aurantioclavine, two building blocks derived from L-tryptophan
CC (PubMed:25571861). The L-tryptophan decarboxylase cnsB converts L-
CC tryptophan to tryptamine, whereas the tryptophan
CC dimethylallyltransferase cnsF converts L-tryptophan to 4-dimethylallyl
CC tryptophan which is further transformed to aurantioclavine by the
CC aurantioclavine synthase cnsA, probably aided by the catalase cnsD
CC (PubMed:25571861). The cytochrome P450 monooxygenase cnsC catalyzes the
CC heterodimeric coupling between the two different indole moieties,
CC tryptamine and aurantioclavine, to construct vicinal quaternary
CC stereocenters and yield the heptacyclic communesin scaffold
CC (PubMed:26963294). The O-methyltransferase cnsE then methylates the
CC communesin scaffold to produce communesin K, the simplest characterized
CC communesin that contains the heptacyclic core (PubMed:25571861). The
CC dioxygenase cnsJ converts communesin K into communesin I
CC (PubMed:25571861). Acylation to introduce the hexadienyl group at
CC position N16 of communesin I by the acyltransferase cnsK leads to the
CC production of communesin B. The hexadienyl group is produced by the
CC highly reducing polyketide synthase cnsI, before being hydrolytically
CC removed from cnsI by the serine hydrolase cnsH, converted into
CC hexadienyl-CoA by the CoA ligase cnsG, and then transferred to
CC communesin I by cnsK (PubMed:25571861). Surprisingly, cnsK may also be
CC a promiscuous acyltransferase that can tolerate a range of acyl groups,
CC including acetyl-, propionyl-, and butyryl-CoA, which lead to
CC communesins A, G and H respectively (PubMed:25571861). The roles of the
CC alpha-ketoglutarate-dependent dioxygenases cnsM and cnsP have still to
CC be determined (PubMed:25571861). {ECO:0000269|PubMed:25571861,
CC ECO:0000269|PubMed:26963294}.
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:25571861}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the biosynthesis of communesins A and B
CC and leads to the accumulation of communesin I, a non-acylated version
CC of communesins A and B. {ECO:0000269|PubMed:25571861}.
CC -!- SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; JQFZ01000090; KGO59704.1; -; Genomic_DNA.
DR RefSeq; XP_016600817.1; XM_016742819.1.
DR AlphaFoldDB; A0A0A2JWD5; -.
DR SMR; A0A0A2JWD5; -.
DR EnsemblFungi; KGO40480; KGO40480; PEXP_030560.
DR EnsemblFungi; KGO50072; KGO50072; PEX1_082110.
DR EnsemblFungi; KGO59704; KGO59704; PEX2_055450.
DR GeneID; 27678238; -.
DR HOGENOM; CLU_026450_1_1_1; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; A0A0A2JWD5; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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..466
FT /note="Communesin N16 acyltransferase cnsK"
FT /id="PRO_0000446466"
SQ SEQUENCE 466 AA; 51273 MW; 2F6DC3C3C3E62D88 CRC64;
MERSLSFEPY LLTPLDHIIK DFYVSSFISF PLHDPTTAVS ALKDGVERLT RALPFLSGAR
VPSSKLPGKR NVMEIHPSPE SLEWIPMLQI KHYRDTTLVA TCSPGPTGCS DLDDSWCALP
IIIPADRPSP VARFRASVFP DGILLCMTLN HAVFDGSGLG TVLKMLATCC CANSAMDHPV
SLPTTYAKEA SSRQIILESA APSSGSDSEA YDRIFKSNDI IPGLDKGITS RRFSFPASKI
RALKDACNAA KPTDQDPAIS RNDVLTALLT ICMTRARQTE QTKNLTTQLA VPVNLRRKFH
PSLPDSYLGN TIIPLVVDID PPTVPSSRCG TSPMHAHLNE LTNLSLRIRK ELKLLDEKDY
TGGLVSYLRE QSDWGATSMK FTDITVSSLR HLDINGLDFG PEIGRANSFD VQSGMYPGIC
DIMPTCGRDR VEDINDVPWD VCVTLEDSAW SAFMEDDLVL WALEKI
