ID   CNSB_PENEN              Reviewed;         454 AA.
AC   A0A0A2IDH4;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=L-tryptophan decarboxylase cnsB {ECO:0000303|PubMed:25571861};
DE            EC=4.1.1.105 {ECO:0000269|PubMed:25571861};
DE   AltName: Full=Communesin biosynthesis cluster protein B {ECO:0000303|PubMed:25571861};
GN   Name=cnsB {ECO:0000303|PubMed:25571861}; ORFNames=PEX2_055360;
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: L-tryptophan decarboxylase; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-tryptophan = CO2 + tryptamine; Xref=Rhea:RHEA:30339,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57887,
CC         ChEBI:CHEBI:57912; EC=4.1.1.105;
CC         Evidence={ECO:0000269|PubMed:25571861};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30340;
CC         Evidence={ECO:0000269|PubMed:25571861};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|RuleBase:RU000382};
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 aurantioclavine.
CC       {ECO:0000269|PubMed:25571861}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; JQFZ01000090; KGO59695.1; -; Genomic_DNA.
DR   RefSeq; XP_016600808.1; XM_016742810.1.
DR   AlphaFoldDB; A0A0A2IDH4; -.
DR   SMR; A0A0A2IDH4; -.
DR   STRING; 27334.A0A0A2IDH4; -.
DR   EnsemblFungi; KGO40471; KGO40471; PEXP_030470.
DR   EnsemblFungi; KGO59695; KGO59695; PEX2_055360.
DR   EnsemblFungi; KGO69145; KGO69145; PEX1_005880.
DR   GeneID; 27678229; -.
DR   HOGENOM; CLU_011856_0_4_1; -.
DR   OrthoDB; 810772at2759; -.
DR   PhylomeDB; A0A0A2IDH4; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0036469; F:L-tryptophan decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..454
FT                   /note="L-tryptophan decarboxylase cnsB"
FT                   /id="PRO_0000446453"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   454 AA;  49883 MW;  896A1A15B0A524E1 CRC64;
     MNSPTASDPI VRTLDAPETK DMQEAFLPGE SPQDVASVIQ ETMDIFDKRM RLTHPHCFCY
     VPSCPSPLAW VGDLFTSLYN VNAVSWDVSS GPSAMEQGMI RWLAQQVGLP PSAGGCFVSG
     GSMANLSAVV AARDKLLPPM RRAEGTIYTS DQTHISIKKC LHIIGFDEHQ IRVIPTDHLF
     RMDTDILRRT IAADRQCGRL PFLVVASCGT TNTGSIDPLH ALADVAEEEG LWLHVDGAYG
     ASIALSDKYR HLVDGIGRAD SISWDGHKWL FQTYGCGIVL TRDSASLAHS FAVDAEYINS
     TTPHGAVNFY NLSPELSRPA RAMPLWFTLR VLGRRQMGEM IDQGFLLART AEEEIRRYPH
     WVILAPVTAS IVVFRYCPLG LKDDDLDTLN LALSARLLAE NVASILTTNI RGRVALRFCA
     TNPATQADTI TKVVQQMDQM ANTMPTCGLG MCKE