CNSJ_PENEN
ID CNSJ_PENEN Reviewed; 333 AA.
AC A0A0A2JYK3;
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=Dioxygenase cnsJ {ECO:0000303|PubMed:25571861};
DE EC=1.14.11.- {ECO:0000269|PubMed:25571861};
DE AltName: Full=Communesin biosynthesis cluster protein J {ECO:0000303|PubMed:25571861};
GN Name=cnsJ {ECO:0000303|PubMed:25571861}; ORFNames=PEX2_055440;
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: Dioxygenase; part of the gene cluster that mediates the
CC biosynthesis of communesins, a prominent class of indole alkaloids with
CC great potential as pharmaceuticals (PubMed:25571861). Communesins are
CC biosynthesized by the coupling of tryptamine and aurantioclavine, two
CC building blocks derived from L-tryptophan (PubMed:25571861). The L-
CC tryptophan decarboxylase cnsB converts L-tryptophan to tryptamine,
CC whereas the tryptophan dimethylallyltransferase cnsF converts L-
CC tryptophan to 4-dimethylallyl tryptophan which is further transformed
CC to aurantioclavine by the aurantioclavine synthase cnsA, probably aided
CC by the catalase cnsD (PubMed:25571861). The cytochrome P450
CC monooxygenase cnsC catalyzes the heterodimeric coupling between the two
CC different indole moieties, tryptamine and aurantioclavine, to construct
CC vicinal quaternary stereocenters and yield the heptacyclic communesin
CC scaffold (PubMed:26963294). The O-methyltransferase cnsE then
CC methylates the communesin scaffold to produce communesin K, the
CC simplest characterized communesin that contains the heptacyclic core
CC (PubMed:25571861). The dioxygenase cnsJ converts communesin K into
CC communesin I (PubMed:25571861). Acylation to introduce the hexadienyl
CC group at position N16 of communesin I by the acyltransferase cnsK leads
CC to the production of communesin B. The hexadienyl group is produced by
CC the highly reducing polyketide synthase cnsI, before being
CC hydrolytically removed from cnsI by the serine hydrolase cnsH,
CC converted into hexadienyl-CoA by the CoA ligase cnsG, and then
CC transferred to communesin I by cnsK (PubMed:25571861). Surprisingly,
CC cnsK may also be a promiscuous acyltransferase that can tolerate a
CC range of acyl groups, including acetyl-, propionyl-, and butyryl-CoA,
CC which lead to communesins A, G and H respectively (PubMed:25571861).
CC The roles of the alpha-ketoglutarate-dependent dioxygenases cnsM and
CC cnsP have still to be determined (PubMed:25571861).
CC {ECO:0000269|PubMed:25571861, ECO:0000269|PubMed:26963294}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q4WAW9};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:25571861}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the biosynthesis of communesin B and
CC leads to the accumulation of communesins F, J and K.
CC {ECO:0000269|PubMed:25571861}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; JQFZ01000090; KGO59703.1; -; Genomic_DNA.
DR RefSeq; XP_016600816.1; XM_016742818.1.
DR AlphaFoldDB; A0A0A2JYK3; -.
DR SMR; A0A0A2JYK3; -.
DR STRING; 27334.A0A0A2JYK3; -.
DR EnsemblFungi; KGO40479; KGO40479; PEXP_030550.
DR EnsemblFungi; KGO50071; KGO50071; PEX1_082100.
DR EnsemblFungi; KGO59703; KGO59703; PEX2_055440.
DR GeneID; 27678237; -.
DR HOGENOM; CLU_047725_0_1_1; -.
DR OrthoDB; 623398at2759; -.
DR PhylomeDB; A0A0A2JYK3; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..333
FT /note="Dioxygenase cnsJ"
FT /id="PRO_0000446465"
FT REGION 309..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
SQ SEQUENCE 333 AA; 37260 MW; 9576BF2F2AC5FED7 CRC64;
MTVDTAPQSH YQETKVSEIP IVILKSSATD DVAAHEAIEA LKVAGVCIVR NLLDRSTVDK
VRQELQPYDK QADSFEGFPK NYCQVAGLLS KSPTYAHSIV GNKLFTAVRN YFLTSTYECW
AEKGTWMSVK SPPQLDSTLA LYVNPGSGDQ GLHRDDATQQ NWNSGASEYS LGRDSGCAMM
VALTECARED GTTRFIPGSH LWDYQYDHPS NDDPRIRYAE MRPGDAYLML SSVIHAGSVN
YSTDRRRVLA AVFAARSHLR QVENQYLTYD IETVRTFPTW LQRFMGYSLS KLFQGWVDKK
DPLLVVDPNA QPEGEDDGGM KPNEGEHVVE AQI
