PAXD_PENPX
ID PAXD_PENPX Reviewed; 438 AA.
AC Q9C451;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Indole diterpene prenyltransferase paxD {ECO:0000303|PubMed:24038699};
DE EC=2.5.1.- {ECO:0000269|PubMed:24038699, ECO:0000305|PubMed:23525886};
DE AltName: Full=Paxilline synthesis protein D {ECO:0000303|PubMed:11169115};
GN Name=paxD {ECO:0000303|PubMed:11169115};
OS Penicillium paxilli.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=70109 {ECO:0000312|EMBL:AAK11526.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=PN2013;
RX PubMed=11169115; DOI=10.1046/j.1365-2958.2001.02265.x;
RA Young C., McMillan L., Telfer E., Scott B.;
RT "Molecular cloning and genetic analysis of an indole-diterpene gene cluster
RT from Penicillium paxilli.";
RL Mol. Microbiol. 39:754-764(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=PN2013;
RX PubMed=23949005; DOI=10.3390/toxins5081422;
RA Scott B., Young C.A., Saikia S., McMillan L.K., Monahan B.J., Koulman A.,
RA Astin J., Eaton C.J., Bryant A., Wrenn R.E., Finch S.C., Tapper B.A.,
RA Parker E.J., Jameson G.B.;
RT "Deletion and gene expression analyses define the paxilline biosynthetic
RT gene cluster in Penicillium paxilli.";
RL Toxins 5:1422-1446(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23525886; DOI=10.1007/s00253-013-4834-9;
RA Liu C., Noike M., Minami A., Oikawa H., Dairi T.;
RT "Functional analysis of a prenyltransferase gene (paxD) in the paxilline
RT biosynthetic gene cluster.";
RL Appl. Microbiol. Biotechnol. 98:199-206(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24038699; DOI=10.1128/aem.02496-13;
RA Liu C., Minami A., Noike M., Toshima H., Oikawa H., Dairi T.;
RT "Regiospecificities and prenylation mode specificities of the fungal indole
RT diterpene prenyltransferases AtmD and PaxD.";
RL Appl. Environ. Microbiol. 79:7298-7304(2013).
CC -!- FUNCTION: Indole diterpene prenyltransferase; part of the gene cluster
CC that mediates the biosynthesis of paxilline, a mycotoxin that acts as
CC an inhibitor of mammalian maxi-K channels (PubMed:11169115,
CC PubMed:23949005). PaxG, the geranylgeranyl diphosphate (GGPP) synthase
CC is proposed to catalyze the first step in paxilline biosynthesis
CC (PubMed:23949005). Condensation of indole-3-glycerol phosphate with
CC GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by
CC epoxidation and cyclization of this intermediate (by paxM and paxB) to
CC form paspaline (PubMed:23949005). Paspaline is subsequently converted
CC to 13-desoxypaxilline by paxP, the latter being then converted to
CC paxilline by paxQ (PubMed:23949005). Finally paxilline can be mono- and
CC di-prenylated by paxD (PubMed:23949005). {ECO:0000269|PubMed:11169115,
CC ECO:0000269|PubMed:23525886, ECO:0000269|PubMed:23949005}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=106.4 uM for paxilline {ECO:0000269|PubMed:23525886,
CC ECO:0000269|PubMed:24038699};
CC KM=0.57 uM for dimethylallyl diphosphate (DMAPP)
CC {ECO:0000269|PubMed:23525886, ECO:0000269|PubMed:24038699};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:23525886};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:23525886};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23525886, ECO:0000305|PubMed:11169115,
CC ECO:0000305|PubMed:23949005}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; HM171111; AAK11526.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9C451; -.
DR SMR; Q9C451; -.
DR PRIDE; Q9C451; -.
DR KEGG; ag:AAK11526; -.
DR BioCyc; MetaCyc:MON-18640; -.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Transferase.
FT CHAIN 1..438
FT /note="Indole diterpene prenyltransferase paxD"
FT /id="PRO_0000436129"
FT BINDING 80..81
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 438 AA; 50065 MW; 463EB6B1732298F8 CRC64;
MQSDELQIPP WESLAEGLGF SNADEEYWWT VFGQPLNKLM DWADYSTSEK YRVLAFIHRY
VIPTCGPRPK PNGDQYWDTF MGFDHTPIQV SINFYNSKAT VRTGNIPISE ASGTTEDPIN
QKASLDTIAS QRHLVPGHNL RLFKHFTDAF FIPNEEANIL NAELENRTIA MQAVQCMLSY
DFPYRQIQTK VAICPMWKSM QVKRPMGDLM ISSIKDLGID AADYMKSLKV IEDFINSEKA
VQSGAYAIFF AFDTMLTDDY QRTRVKIYFA TQSTAFNNMV DIFTLGGRLD GPEMQRATKE
LRKLWMSTMA IPDGLRDDET LPKSPLPCAG VIFNFEIWPG ADKPNPKIYL PCAYYGKDDL
DIADGMDSFF KDQGWSKSFH SYKDNYIKAF VKDGKVMCRH HDISFSYKGQ GAYITAYYKP
ELSEYADPSV WAPKLFKA
