7DMAW_ASPFU
ID 7DMAW_ASPFU Reviewed; 472 AA.
AC Q4WYG3; A8JY03;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=7-dimethylallyltryptophan synthase {ECO:0000303|PubMed:17906140};
DE Short=7-DMATS {ECO:0000303|PubMed:17906140};
DE EC=2.5.1.80 {ECO:0000269|PubMed:17906140, ECO:0000269|PubMed:18481055};
DE AltName: Full=Tryptophan aminopeptidase {ECO:0000303|PubMed:18635009};
DE EC=3.4.11.17 {ECO:0000269|PubMed:18635009};
GN Name=etpPT; ORFNames=AFUA_3G12930;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=B5233 / ATCC 13073;
RX PubMed=17906140; DOI=10.1099/mic.0.2007/009019-0;
RA Kremer A., Westrich L., Li S.-M.;
RT "A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus:
RT overproduction, purification and biochemical characterization.";
RL Microbiology 153:3409-3416(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=18481055; DOI=10.1007/s00253-008-1505-3;
RA Kremer A., Li S.-M.;
RT "Potential of a 7-dimethylallyltryptophan synthase as a tool for production
RT of prenylated indole derivatives.";
RL Appl. Microbiol. Biotechnol. 79:951-961(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=18635009; DOI=10.1016/j.chembiol.2008.05.019;
RA Kremer A., Li S.-M.;
RT "Tryptophan aminopeptidase activity of several indole prenyltransferases
RT from Aspergillus fumigatus.";
RL Chem. Biol. 15:729-738(2008).
CC -!- FUNCTION: Catalyzes the prenylation of L-tryptophan at the C-7 position
CC of the indole moiety. The enzyme is specific for dimethylallyl
CC diphosphate (DMAPP) as prenyl donor. Accepts also D-tryptophan,
CC typtophan-derivatives with modifications at the side chain or the
CC indole ring, and linear and cyclic dipeptides such as H-L-Trp-L-Gly-OH
CC or cyclo-L-Trp-L-Gly as substrates, however with lower efficiency. Also
CC has tryptophan aminopeptidase activity towards linear peptides with a
CC tryptophanyl moiety at the N-terminus. Dipeptides are better substrates
CC than peptides with 3 or more amino acids. Enzymatic rate constants
CC however are much higher for the prenyltransferase activity than for the
CC aminopeptidase activity. {ECO:0000269|PubMed:17906140,
CC ECO:0000269|PubMed:18481055, ECO:0000269|PubMed:18635009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + L-tryptophan = 7-(3-methylbut-2-
CC enyl)-L-tryptophan + diphosphate; Xref=Rhea:RHEA:30563,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:62497; EC=2.5.1.80;
CC Evidence={ECO:0000269|PubMed:17906140, ECO:0000269|PubMed:18481055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of N-terminal tryptophan.; EC=3.4.11.17;
CC Evidence={ECO:0000269|PubMed:18635009};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:17906140};
CC KM=137 uM for L-tryptophan {ECO:0000269|PubMed:17906140};
CC KM=350 uM for H-L-Trp-L-Gly-OH (for aminopeptidase activity)
CC {ECO:0000269|PubMed:17906140};
CC Vmax=0.21 umol/min/mg enzyme {ECO:0000269|PubMed:17906140};
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; EF539173; ABS89001.1; -; mRNA.
DR EMBL; AAHF01000002; EAL92290.2; -; Genomic_DNA.
DR RefSeq; XP_754328.2; XM_749235.2.
DR AlphaFoldDB; Q4WYG3; -.
DR SMR; Q4WYG3; -.
DR STRING; 330879.Q4WYG3; -.
DR MEROPS; M77.001; -.
DR EnsemblFungi; EAL92290; EAL92290; AFUA_3G12930.
DR GeneID; 3512456; -.
DR KEGG; afm:AFUA_3G12930; -.
DR VEuPathDB; FungiDB:Afu3g12930; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_2_2_1; -.
DR InParanoid; Q4WYG3; -.
DR OMA; GVYMTMY; -.
DR OrthoDB; 1531660at2759; -.
DR BioCyc; MetaCyc:MON-15368; -.
DR BRENDA; 2.5.1.80; 508.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:AspGD.
DR GO; GO:0008233; F:peptidase activity; IDA:AspGD.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:AspGD.
DR GO; GO:0009821; P:alkaloid biosynthetic process; IDA:AspGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IDA:AspGD.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
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 SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Hydrolase; Protease; Reference proteome; Transferase.
FT CHAIN 1..472
FT /note="7-dimethylallyltryptophan synthase"
FT /id="PRO_0000418541"
FT VARIANT 15
FT /note="P -> Q (in strain: B5233 / ATCC 13073)"
FT VARIANT 271
FT /note="E -> G (in strain: B5233 / ATCC 13073)"
SQ SEQUENCE 472 AA; 52688 MW; 9FCA3EA23FB645DE CRC64;
MSIGAEIDSL VPAPPGLNGT AAGYPAKTQK ELSNGDFDAH DGLSLAQLTP YDVLTAALPL
PAPASSTGFW WRETGPVMSK LLAKANYPLY THYKYLMLYH THILPLLGPR PPLENSTHPS
PSNAPWRSFL TDDFTPLEPS WNVNGNSEAQ STIRLGIEPI GFEAGAAADP FNQAAVTQFM
HSYEATEVGA TLTLFEHFRN DMFVGPETYA ALRAKIPEGE HTTQSFLAFD LDAGRVTTKA
YFFPILMSLK TGQSTTKVVS DSILHLALKS EVWGVQTIAA MSVMEAWIGS YGGAAKTEMI
SVDCVNEADS RIKIYVRMPH TSLRKVKEAY CLGGRLTDEN TKEGLKLLDE LWRTVFGIDD
EDAELPQNSH RTAGTIFNFE LRPGKWFPEP KVYLPVRHYC ESDMQIASRL QTFFGRLGWH
NMEKDYCKHL EDLFPHHPLS SSTGTHTFLS FSYKKQKGVY MTMYYNLRVY ST
