TDIE_EMENI
ID TDIE_EMENI Reviewed; 317 AA.
AC A7XRZ1; C8VEN6; Q5AT60;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Probable methyltransferase tdiE {ECO:0000303|PubMed:17704773};
DE EC=2.1.1.- {ECO:0000305|PubMed:17704773};
DE AltName: Full=Terrequinone biosynthesis protein D {ECO:0000303|PubMed:16426969};
GN Name=tdiE {ECO:0000303|PubMed:16426969}; ORFNames=AN8517;
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 [MRNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=17704773; DOI=10.1038/nchembio.2007.20;
RA Balibar C.J., Howard-Jones A.R., Walsh C.T.;
RT "Terrequinone A biosynthesis through L-tryptophan oxidation, dimerization
RT and bisprenylation.";
RL Nat. Chem. Biol. 3:584-592(2007).
RN [2]
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 [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
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 [4]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=16426969; DOI=10.1016/j.chembiol.2005.10.008;
RA Bok J.W., Hoffmeister D., Maggio-Hall L.A., Murillo R., Glasner J.D.,
RA Keller N.P.;
RT "Genomic mining for Aspergillus natural products.";
RL Chem. Biol. 13:31-37(2006).
RN [5]
RP IDENTIFICATION, INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17291795; DOI=10.1016/j.fgb.2006.12.010;
RA Bouhired S., Weber M., Kempf-Sontag A., Keller N.P., Hoffmeister D.;
RT "Accurate prediction of the Aspergillus nidulans terrequinone gene cluster
RT boundaries using the transcriptional regulator LaeA.";
RL Fungal Genet. Biol. 44:1134-1145(2007).
RN [6]
RP FUNCTION.
RX PubMed=18029206; DOI=10.1016/j.fgb.2007.09.004;
RA Schneider P., Weber M., Hoffmeister D.;
RT "The Aspergillus nidulans enzyme TdiB catalyzes prenyltransfer to the
RT precursor of bioactive asterriquinones.";
RL Fungal Genet. Biol. 45:302-309(2008).
RN [7]
RP FUNCTION.
RX PubMed=22083274; DOI=10.1007/s00253-011-3657-9;
RA Sakai K., Kinoshita H., Nihira T.;
RT "Heterologous expression system in Aspergillus oryzae for fungal
RT biosynthetic gene clusters of secondary metabolites.";
RL Appl. Microbiol. Biotechnol. 93:2011-2022(2012).
RN [8]
RP INDUCTION.
RX PubMed=26773375; DOI=10.1016/j.fgb.2016.01.004;
RA Bayram O., Feussner K., Dumkow M., Herrfurth C., Feussner I., Braus G.H.;
RT "Changes of global gene expression and secondary metabolite accumulation
RT during light-dependent Aspergillus nidulans development.";
RL Fungal Genet. Biol. 87:30-53(2016).
CC -!- FUNCTION: Probable methyltransferase; part of the gene cluster that
CC mediates the biosynthesis of terrequinone A, an antitumor agent
CC (PubMed:17704773, PubMed:16426969, PubMed:17291795, PubMed:22083274).
CC The first step in the biosynthetic pathway for terrequinone A is
CC formation of indole pyruvic acid (IPA) from L-tryptophan by the
CC aminotransferase tdiD (PubMed:17704773). The nonribosomal peptide
CC synthase tdiA then immediately converts unstable IPA to
CC didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA
CC molecules (PubMed:17704773). The symmetric connectivity of the 2 IPA
CC molecules is thought to arise by head-to-tail dual Claisen
CC condensations facilitated by the TE domain (PubMed:17704773). TdiB then
CC catalyzes reverse prenylation by transferring dimethylallyl diphosphate
CC to carbon atom 2' of DDAQ D, to yield asterriquinone C-1
CC (PubMed:18029206). Finally, tdiC and tdiE enzymes robustly convert
CC asterriquinone C-1 to terrequinone A via a transformation involving
CC regular prenylation at carbon atom 5, which requires elimination of the
CC hydroxy group on C-5 (PubMed:17704773, PubMed:18029206).
CC {ECO:0000269|PubMed:16426969, ECO:0000269|PubMed:17291795,
CC ECO:0000269|PubMed:17704773, ECO:0000269|PubMed:18029206,
CC ECO:0000269|PubMed:22083274}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:17291795, ECO:0000269|PubMed:17704773}.
CC -!- INDUCTION: Expressed during both sexual and asexual development
CC (PubMed:26773375). Expression is positively regulated by the secondary
CC metabolism regulator laeA (PubMed:16426969, PubMed:17291795).
CC {ECO:0000269|PubMed:16426969, ECO:0000269|PubMed:17291795,
CC ECO:0000269|PubMed:26773375}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of terrequinone A
CC (PubMed:17291795). {ECO:0000269|PubMed:17291795}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LaeA
CC methyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF80718.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA66861.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA66873.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF550585; ABU51606.1; -; mRNA.
DR EMBL; BN001305; CBF80718.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000154; EAA66861.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000155; EAA66873.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_681786.1; XM_676694.1.
DR RefSeq; XP_681789.1; XM_676697.1.
DR AlphaFoldDB; A7XRZ1; -.
DR EnsemblFungi; EAA66861; EAA66861; AN8517.2.
DR EnsemblFungi; EAA66873; EAA66873; AN8520.2.
DR GeneID; 2868673; -.
DR GeneID; 2868783; -.
DR KEGG; ani:AN8517.2; -.
DR KEGG; ani:AN8520.2; -.
DR VEuPathDB; FungiDB:AN8520; -.
DR OrthoDB; 1047281at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IDA:AspGD.
DR GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
DR GO; GO:1900796; P:terrequinone A biosynthetic process; IMP:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..317
FT /note="Probable methyltransferase tdiE"
FT /id="PRO_0000436368"
SQ SEQUENCE 317 AA; 35718 MW; 509AB9B5D7332999 CRC64;
MVNRPYANMN DLANAVAESV QKYLDNSGQA RNGLFQKTNN GERDIETERL ALQHQLFHLT
LDGKLQLSPL PSPVQSVLDI ATGDSTWVHA FAEQNPSAYI VANDPSPTSK IPLGLSVIPD
ASDANEPWTY TRQFDFVHCR QHHRRLDEPR LFKQAFSSLT PGGWLEMQEL SNPVTSDDGT
LSENNPLSQW GRLLIEASKK MNRPVDNPAK YETWMREAGF VNCHTVAYNW PTNPWPADEK
GKTLGLWNLY NVLQRFEEFS VALLVKVLGW EMDDAKTFLG NVKEELMNEG VHGYWPVYVV
YGQKPAAPGS DVITDSE
