TDIB_EMENI
ID TDIB_EMENI Reviewed; 419 AA.
AC A7XRY3; C8VEN3; Q5AT66;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Indole prenyltransferase tdiB {ECO:0000303|PubMed:18029206};
DE EC=2.5.1.- {ECO:0000269|PubMed:18029206};
DE AltName: Full=Terrequinone biosynthesis protein B {ECO:0000303|PubMed:16426969};
GN Name=tdiB {ECO:0000303|PubMed:16426969}; ORFNames=AN8514;
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, AND FUNCTION.
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 INDUCTION.
RX PubMed=18378656; DOI=10.1128/aem.02842-07;
RA Atoui A., Bao D., Kaur N., Grayburn W.S., Calvo A.M.;
RT "Aspergillus nidulans natural product biosynthesis is regulated by mpkB, a
RT putative pheromone response mitogen-activated protein kinase.";
RL Appl. Environ. Microbiol. 74:3596-3600(2008).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
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 [8]
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 [9]
RP INDUCTION.
RX PubMed=24066102; DOI=10.1371/journal.pone.0074122;
RA Ramamoorthy V., Dhingra S., Kincaid A., Shantappa S., Feng X., Calvo A.M.;
RT "The putative C2H2 transcription factor MtfA is a novel regulator of
RT secondary metabolism and morphogenesis in Aspergillus nidulans.";
RL PLoS ONE 8:E74122-E74122(2013).
RN [10]
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: Indole prenyltransferase; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=73.80 uM for didemethylasterriquinone D (DDAQ D)
CC {ECO:0000269|PubMed:18029206};
CC KM=19.88 uM for dimethylallyl diphosphate (DMAPP)
CC {ECO:0000269|PubMed:18029206};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:17291795, ECO:0000269|PubMed:17704773}.
CC -!- INDUCTION: Specifically expressed at both asexual stages
CC (PubMed:26773375). Expression is positively regulated by the secondary
CC metabolism regulator laeA (PubMed:16426969, PubMed:17291795).
CC Expression is also positively regulated by mpkB (PubMed:18378656).
CC Expression is also positively regulated by mtfA (PubMed:24066102).
CC {ECO:0000269|PubMed:16426969, ECO:0000269|PubMed:17291795,
CC ECO:0000269|PubMed:18378656, ECO:0000269|PubMed:24066102,
CC ECO:0000269|PubMed:26773375}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of terrequinone A
CC (PubMed:18029206). {ECO:0000269|PubMed:18029206}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; EF550582; ABU51603.1; -; mRNA.
DR EMBL; BN001305; CBF80712.1; -; Genomic_DNA.
DR EMBL; AACD01000154; EAA66858.1; -; Genomic_DNA.
DR RefSeq; XP_681783.1; XM_676691.1.
DR AlphaFoldDB; A7XRY3; -.
DR SMR; A7XRY3; -.
DR STRING; 162425.CADANIAP00003006; -.
DR EnsemblFungi; CBF80712; CBF80712; ANIA_08514.
DR EnsemblFungi; EAA66858; EAA66858; AN8514.2.
DR GeneID; 2868862; -.
DR KEGG; ani:AN8514.2; -.
DR VEuPathDB; FungiDB:AN8514; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR OMA; HNEPEPY; -.
DR OrthoDB; 1531660at2759; -.
DR BioCyc; MetaCyc:MON-18728; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:AspGD.
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; IDA:AspGD.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..419
FT /note="Indole prenyltransferase tdiB"
FT /id="PRO_0000436365"
FT BINDING 58..59
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 419 AA; 45993 MW; 9EFB4F68925BD909 CRC64;
MATEYWSRHL RSVLAPLFAA AGTYSPEDQE SHLAFIDEHI APNLGPLPWE PHGPYSTPSS
LVGSPFDPSI NIVSSGKAKV RFDFDVISPP DRTGPDPFAE GSAREILHRL ADLVGADTQW
MGYLMDALYL TPAEAEVAKT KLPPGVAIPP SSVGFDFDGP ERTLKFYIPS VRKALATGQD
VSELMLKTLR GLQPLGSELV PAMDLIASYL STRTNDAMLP LVGIDCLDPR THKNARVKCY
LHTSSNSFAV VRDVLTLGGR LSDDTSLKRV ETLKSVWPLL INELEGPQSD AATMDESWSK
PERLNRTGYS GIQYTIEITP GQAIPDTKIY VPLFQYTDSS EVAERNFESA LKKLGNEWGL
SGKYRSVMQE IFKDVENYGQ TYASFSYTEG KGVYTTSYVA MPIKDEGGGS LAGDFGFRN
