PTF_SCLS1
ID PTF_SCLS1 Reviewed; 309 AA.
AC A7EVV6; A0A1D9QLA6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=SS1G_09465;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
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=ATCC 18683 / 1980 / Ss-1;
RX PubMed=28204478; DOI=10.1093/gbe/evx030;
RA Derbyshire M., Denton-Giles M., Hegedus D., Seifbarghy S., Rollins J.,
RA van Kan J., Seidl M.F., Faino L., Mbengue M., Navaud O., Raffaele S.,
RA Hammond-Kosack K., Heard S., Oliver R.;
RT "The complete genome sequence of the phytopathogenic fungus Sclerotinia
RT sclerotiorum reveals insights into the genome architecture of broad host
RT range pathogens.";
RL Genome Biol. Evol. 9:593-618(2017).
RN [3]
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=1232 uM for DMAPP {ECO:0000269|PubMed:20351110};
CC KM=590 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; CH476633; EDN93598.1; -; Genomic_DNA.
DR EMBL; CP017828; APA15717.1; -; Genomic_DNA.
DR RefSeq; XP_001589743.1; XM_001589693.1.
DR EnsemblFungi; EDN93598; EDN93598; SS1G_09465.
DR GeneID; 5485694; -.
DR KEGG; ssl:SS1G_09465; -.
DR VEuPathDB; FungiDB:sscle_15g104870; -.
DR eggNOG; ENOG502SMTG; Eukaryota.
DR HOGENOM; CLU_057184_0_0_1; -.
DR InParanoid; A7EVV6; -.
DR OMA; ALNYRFY; -.
DR OrthoDB; 971902at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR Proteomes; UP000177798; Chromosome 15.
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_0000455463"
SQ SEQUENCE 309 AA; 34721 MW; 75E5439230B5AAD1 CRC64;
MVVQLISKPS KFSQSRFLDD IRNLSAAINA PYSERTTIEA LSVYSHSFHN GVVLWRVTDR
PGDALNYRFY SREPIDTVSI AASAGLLSPD IANTLGKLVT SWSSLYDGTP EESCDFDAEK
GLVKAWVYFG GMRPLDDILG AEGVPESVRQ HEKRFKELGL QKVRHVAVDY HKQTVNLYFR
AQGPISFQQA TAFNALAGAE PPSQSQFIEM REFLNAVGYT FAVTINIDSG DIERVGYYAL
KLPERSAKKW PAINAQLERF VQFAPSYDRE EMNAVAWSFG ERKTYVKFER SYCGELIPLI
KGWGTTLSS
