PTF_BOTFB
ID PTF_BOTFB Reviewed; 309 AA.
AC A0A384JK99;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Aromatic prenyltransferase {ECO:0000303|PubMed:20351110};
DE EC=2.5.1.- {ECO:0000269|PubMed:20351110};
GN Name=ptf {ECO:0000303|PubMed:20351110}; ORFNames=BCIN_06g02600;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=23104368; DOI=10.1128/ec.00164-12;
RA Staats M., van Kan J.A.L.;
RT "Genome update of Botrytis cinerea strains B05.10 and T4.";
RL Eukaryot. Cell 11:1413-1414(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=26913498; DOI=10.1111/mpp.12384;
RA van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L.,
RA Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D.,
RA Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.;
RT "A gapless genome sequence of the fungus Botrytis cinerea.";
RL Mol. Plant Pathol. 18:75-89(2017).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=20351110; DOI=10.1074/jbc.m110.113720;
RA Haug-Schifferdecker E., Arican D., Brueckner R., Heide L.;
RT "A new group of aromatic prenyltransferases in fungi, catalyzing a 2,7-
RT dihydroxynaphthalene 3-dimethylallyl-transferase reaction.";
RL J. Biol. Chem. 285:16487-16494(2010).
CC -!- FUNCTION: Prenyltransferase that attaches isoprenoid moieties to carbon
CC atoms of aromatic substrates in an enzyme-catalyzed Friedel-Crafts
CC reaction (PubMed:20351110). Shows specificity for dimethylallyl
CC diphosphate (DMAPP) and does not accept geranyl diphosphate (GPP) or
CC isopentenyl diphosphate (IPP) (PubMed:20351110). Prenylates the
CC artificial substrate 2,7-dihydroxynaphthalene (2,7-DHN), as well as
CC dihydrophenazine-1-carboxylic acid and 4-hydroxybenzoic acid at lower
CC levels (PubMed:20351110). Only traces of products are detected with
CC aspulvinone E or flaviolin as substrates; and no product is formed with
CC L-tryptophan, L-tyrosine, or 4-hydroxyphenylpyruvate (PubMed:20351110).
CC Ptf seems no to be involved in the prenylation reaction in the
CC biosynthesis of aspulvinone H and J and the physiological function of
CC ptf remains unknown (PubMed:20351110). {ECO:0000269|PubMed:20351110}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1010 uM for DMAPP {ECO:0000269|PubMed:20351110};
CC KM=996 uM for 2,7-dihydroxynaphthalene {ECO:0000269|PubMed:20351110};
CC -!- MISCELLANEOUS: The gene is not located within a recognizable secondary
CC metabolic gene cluster. {ECO:0000269|PubMed:20351110}.
CC -!- SIMILARITY: Belongs to the aromatic prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CP009810; ATZ50774.1; -; Genomic_DNA.
DR RefSeq; XP_001560463.1; XM_001560413.1.
DR GeneID; 5441104; -.
DR KEGG; bfu:BCIN_06g02600; -.
DR VEuPathDB; FungiDB:Bcin06g02600; -.
DR OMA; ALNYRFY; -.
DR Proteomes; UP000001798; Chromosome bcin06.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR CDD; cd13931; PT-CloQ_NphB; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR020965; Prenyltransferase_CloQ.
DR InterPro; IPR036239; PrenylTrfase-like_sf.
DR Pfam; PF11468; PTase_Orf2; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR SFLD; SFLDG01163; II; 1.
DR SUPFAM; SSF143492; SSF143492; 1.
PE 1: Evidence at protein level;
KW Prenyltransferase; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="Aromatic prenyltransferase"
FT /id="PRO_0000455462"
SQ SEQUENCE 309 AA; 34474 MW; 434F9267B029F90A CRC64;
MVVQAVSESL KFDQSRFLND IQILSAAINA PYSESTTKKV LSVFSDSFHD GVVLWRATDR
VGDALNYRFY SRRPIDTVTI ASSAGLLSPD VVSNLGRLVT SWSSLYDGLP EESCDFDAEK
GLVKAWVYMR GMRPLGDILS AEGVPESLKQ HEERFKALEL EKVRHVAVDY QKATVNLYFR
AQGPISLQQA TSFNALAGAG PPSQTQFLEM QEFLNAVGYT FAVTIRVDSG DIERVGYYAL
KLPDRATKNW PVINAQLEKF AQFAPSYDRE EMNAVAWSFG GTKRYVKFER SYCGELVPLI
KGWGTTLSS
