TDID_EMENI
ID TDID_EMENI Reviewed; 436 AA.
AC A7XRY8; C8VEN5; Q5AT61; Q5AT64;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Aminotransferase tdiD {ECO:0000305};
DE EC=2.6.1.- {ECO:0000269|PubMed:17704773};
DE AltName: Full=Terrequinone biosynthesis protein D {ECO:0000303|PubMed:16426969};
GN Name=tdiD {ECO:0000303|PubMed:16426969}; ORFNames=AN8516;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 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).
CC -!- FUNCTION: Aminotransferase; part of the gene cluster that mediates the
CC biosynthesis of terrequinone A, an antitumor agent (PubMed:17704773,
CC PubMed:16426969, PubMed:17291795, PubMed:22083274). The first step in
CC the biosynthetic pathway for terrequinone A is formation of indole
CC pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD
CC (PubMed:17704773). The nonribosomal peptide synthase tdiA then
CC immediately converts unstable IPA to didemethylasterriquinone D (DDAQ
CC D), via condensation of 2 IPA molecules (PubMed:17704773). The
CC symmetric connectivity of the 2 IPA molecules is thought to arise by
CC head-to-tail dual Claisen condensations facilitated by the TE domain
CC (PubMed:17704773). TdiB then catalyzes reverse prenylation by
CC transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to
CC yield asterriquinone C-1 (PubMed:18029206). Finally, tdiC and tdiE
CC enzymes robustly convert asterriquinone C-1 to terrequinone A via a
CC transformation involving regular prenylation at carbon atom 5, which
CC requires elimination of the hydroxy group on C-5 (PubMed:17704773,
CC PubMed:18029206). {ECO:0000269|PubMed:16426969,
CC ECO:0000269|PubMed:17291795, ECO:0000269|PubMed:17704773,
CC ECO:0000269|PubMed:18029206, ECO:0000269|PubMed:22083274}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17704773};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=198 uM for L-tryptophan {ECO:0000269|PubMed:17704773};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:17291795, ECO:0000269|PubMed:17704773}.
CC -!- INDUCTION: 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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF80716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA66860.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA66872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF550584; ABU51605.1; -; mRNA.
DR EMBL; BN001305; CBF80716.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000154; EAA66860.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000155; EAA66872.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_681785.1; XM_676693.1.
DR RefSeq; XP_681788.1; XM_676696.1.
DR AlphaFoldDB; A7XRY8; -.
DR SMR; A7XRY8; -.
DR STRING; 162425.CADANIAP00003008; -.
DR PRIDE; A7XRY8; -.
DR EnsemblFungi; EAA66860; EAA66860; AN8516.2.
DR EnsemblFungi; EAA66872; EAA66872; AN8519.2.
DR GeneID; 2868782; -.
DR GeneID; 2868787; -.
DR KEGG; ani:AN8516.2; -.
DR KEGG; ani:AN8519.2; -.
DR eggNOG; KOG0634; Eukaryota.
DR OrthoDB; 1241781at2759; -.
DR BioCyc; MetaCyc:MON-18726; -.
DR BRENDA; 2.6.1.28; 517.
DR SABIO-RK; A7XRY8; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR GO; GO:1900796; P:terrequinone A biosynthetic process; IMP:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..436
FT /note="Aminotransferase tdiD"
FT /id="PRO_0000436367"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Z0"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Z0"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Z0"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Z0"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Z0"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5Z0"
SQ SEQUENCE 436 AA; 47705 MW; 015F606F1A48EDD8 CRC64;
MGSIGANNAV ADPTPLFSSR VQKWEPGAIR SLLPLEALPG MISLVAGKPS PETFPIAEIA
ISLKDTPAGT GRIVVDGDEL NQALQYGLPR GNAQLIQWFE SLQRSVHGLD ENGGWSCCIG
NGSQELIHRV IQVFTDPGDP VLLETPAYPG VAGFLRADGQ ELIPVYSDAQ GLNPASLEQA
LSEWPGDSPR PKVLYTTPTG SNPTGQSCTE SRKAEILRLA KRFNFIILED DAYYYLNYGD
DKQRARSYLA LERDVNGESG RVVRFDSLSK IVSPGMRLGI LTAQAAVVDK VVRITENINL
QPSSTTQLLA LSLLRHWGQA GFLKHCAEAA EVYRRRRDVF VSAAERHLQG RATWVVPTAG
MFVWLELKLP PEMDSFELLK SQGMKNGVLA IPGVAFMPGN EQTCYIRVSF SLVPERDMDE
ACRRIAGLVD RCACHS
