ID   CNSD_PENEN              Reviewed;         465 AA.
AC   A0A0A2JW88;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Catalase cnsD {ECO:0000303|PubMed:25571861};
DE            EC=1.11.-.- {ECO:0000305|PubMed:25571861};
DE   AltName: Full=Communesin biosynthesis cluster protein D {ECO:0000303|PubMed:25571861};
GN   Name=cnsD {ECO:0000303|PubMed:25571861}; ORFNames=PEX2_055380;
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, AND 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: Catalase; 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=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P15202};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305|PubMed:25571861}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; JQFZ01000090; KGO59697.1; -; Genomic_DNA.
DR   RefSeq; XP_016600810.1; XM_016742812.1.
DR   AlphaFoldDB; A0A0A2JW88; -.
DR   SMR; A0A0A2JW88; -.
DR   STRING; 27334.A0A0A2JW88; -.
DR   EnsemblFungi; KGO40473; KGO40473; PEXP_030490.
DR   EnsemblFungi; KGO50065; KGO50065; PEX1_082040.
DR   EnsemblFungi; KGO59697; KGO59697; PEX2_055380.
DR   GeneID; 27678231; -.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   OrthoDB; 507937at2759; -.
DR   PhylomeDB; A0A0A2JW88; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..465
FT                   /note="Catalase cnsD"
FT                   /id="PRO_0000446459"
FT   ACT_SITE        39
FT                   /evidence="ECO:0000250|UniProtKB:P15202"
FT   BINDING         331
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P15202"
SQ   SEQUENCE   465 AA;  52868 MW;  F8392E342C577784 CRC64;
     MERSGTTPRF AQNPVVNDTG LLEALSHFNR EKIPERVVHA KGTGAYGEFE VTDDISDICN
     IDMLLGVGKK TPCVGRFSTT GLERGSAEGI RDVKGLGLKF DTKEGNWDWV CINFPYFFIR
     DPAKFPDLMH AQQRDPKTNL LNPNMYWDWV ADNPESLHLV LTLFSKLGTM FNWRTMSAYL
     GHAYKWTMPD GSFKYVHVYL SPNGGPSNEN ASMDDAMDEN INDPDGASRD LYEAIERGDF
     PTWTAYAQVV DPEDAPDLDF NILDMTKHWN YGFYPKNGSV IPKRAFGTLT LNRNPEKYFS
     EIECLTFSPS NLVPGVLPSE DPILQARMFA YPDAQRYRLG VNPENPPARP KKPLSLKPGS
     QKFDEWVSQV SSPAWSEAKE DDYEFARELY EWYPQFRDQE FQNELIDNLA ESISQTCDAV
     RQKVYRTFAL VSTDLADRVR EGVEKRLETA ATNSTPQELP GRARL