NPTA_EMENI
ID NPTA_EMENI Reviewed; 434 AA.
AC C8VEJ5;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Tryptophan dimethylallyltransferase nptA {ECO:0000305};
DE EC=2.5.1.34 {ECO:0000269|PubMed:23248299};
DE AltName: Full=4-dimethylallyltryptophan synthase nptA {ECO:0000303|PubMed:23248299};
DE Short=DMATS nptA {ECO:0000303|PubMed:23248299};
DE AltName: Full=Nidulanin A prenyltransferase {ECO:0000305};
GN Name=nptA {ECO:0000303|PubMed:23248299}; ORFNames=ANIA_11080;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000312|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=23248299; DOI=10.1073/pnas.1205532110;
RA Andersen M.R., Nielsen J.B., Klitgaard A., Petersen L.M., Zachariasen M.,
RA Hansen T.J., Blicher L.H., Gotfredsen C.H., Larsen T.O., Nielsen K.F.,
RA Mortensen U.H.;
RT "Accurate prediction of secondary metabolite gene clusters in filamentous
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E99-E107(2013).
CC -!- FUNCTION: Nonribosomal peptide synthase involved in the synthesis of
CC nidulanin A and derived compounds (PubMed:23248299). Nidulanin A is a
CC tetracyclopeptide with the sequence L-Phe-L-Kyn-L-Val-D-Val and an
CC isoprene unit N-linked to the amino group of L-kynurenine
CC (PubMed:23248299). The NRPS nlsA is responsible of the synthesis of the
CC cyclopeptide and the prenyltransferase nptA adds the isoprene unit on
CC the L-kynurenine residue of nidulanin A (PubMed:23248299). Further
CC modifications lead to additional oxygenated related compounds
CC (PubMed:23248299). {ECO:0000269|PubMed:23248299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + L-tryptophan = 4-(3-methylbut-2-
CC enyl)-L-tryptophan + diphosphate; Xref=Rhea:RHEA:14173,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57912,
CC ChEBI:CHEBI:58209; EC=2.5.1.34;
CC Evidence={ECO:0000269|PubMed:23248299};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23248299}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q50EL0}.
CC -!- DISRUPTION PHENOTYPE: Accumulates the unprenylated precursor of
CC nidulanin A, but none of the three prenylated forms, including
CC nidulanin A and two oxygenated related compounds (PubMed:23248299).
CC {ECO:0000269|PubMed:23248299}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001305; CBF80641.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VEJ5; -.
DR SMR; C8VEJ5; -.
DR EnsemblFungi; CBF80641; CBF80641; ANIA_11080.
DR VEuPathDB; FungiDB:AN11080; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_0_0_1; -.
DR InParanoid; C8VEJ5; -.
DR OMA; CLDNTID; -.
DR OrthoDB; 1531660at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0050364; F:tryptophan dimethylallyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..434
FT /note="Tryptophan dimethylallyltransferase nptA"
FT /id="PRO_0000444199"
FT BINDING 91..92
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 100
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 206
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 434 AA; 48915 MW; 13461F1CA99E4BE9 CRC64;
MVATPDDPRA QTIVDLFNGQ GSAPAPFDVL TSALSFPTRD QEQWWRKTGP MFGQMLASSG
YTLDQQYRHL TFYYNQLVPR LGPHPATFHS SLTVSGLPME FSINYQQKGA HPMVRIGAEP
IDSFSGTERD PFNQIPPAEM VNHFSRAGVK GFDPELYAYF EPKHSLTREQ QARLPKEVPG
GDKLKTQYAF GFDFKGDEVS LKGYSYPGLK ATMAGQEVAK LVGDGVKDLK NQGKLDCTEA
WAAVEAYMTE LNGWGYHNLW AWDYVSPAKS RLKFYSFVMD VVDKTKLEEL WTLNGRATSP
AHQEGLRHLK ELWDIIDLKN VGKRDLPADA PQIPEDAAPM VWNYEMTAGN PLPFGKGYFP
LQGLNDAGCI QKLVKFFELM GWKDLAAKYP ETIQSFYPGL DLSKTSHLLM WVSYTYSEKT
GVYLSIYNHP CPEK
