ID   TDIC_EMENI              Reviewed;         355 AA.
AC   A7XRY6; C8VEN4; Q5AT62;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable NADPH-dependent quinone reductase tdiC {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000305|PubMed:17704773};
DE   AltName: Full=Terrequinone biosynthesis protein C {ECO:0000303|PubMed:16426969};
GN   Name=tdiC {ECO:0000303|PubMed:16426969}; ORFNames=AN8515;
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   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 NADPH-dependent quinone reductase; part of the gene
CC       cluster that mediates the biosynthesis of terrequinone A, an antitumor
CC       agent (PubMed:17704773, PubMed:16426969, PubMed:17291795,
CC       PubMed:22083274). The first step in the biosynthetic pathway for
CC       terrequinone A is formation of indole pyruvic acid (IPA) from L-
CC       tryptophan by the aminotransferase tdiD (PubMed:17704773). The
CC       nonribosomal peptide synthase tdiA then immediately converts unstable
CC       IPA to 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   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783; Evidence={ECO:0000305};
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   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; EF550583; ABU51604.1; -; mRNA.
DR   EMBL; BN001305; CBF80714.1; -; Genomic_DNA.
DR   EMBL; AACD01000154; EAA66859.1; -; Genomic_DNA.
DR   EMBL; AACD01000155; EAA66871.1; -; Genomic_DNA.
DR   RefSeq; XP_681784.1; XM_676692.1.
DR   RefSeq; XP_681787.1; XM_676695.1.
DR   AlphaFoldDB; A7XRY6; -.
DR   SMR; A7XRY6; -.
DR   STRING; 162425.CADANIAP00003007; -.
DR   EnsemblFungi; CBF80714; CBF80714; ANIA_08518.
DR   EnsemblFungi; EAA66859; EAA66859; AN8515.2.
DR   EnsemblFungi; EAA66871; EAA66871; AN8518.2.
DR   GeneID; 2868654; -.
DR   GeneID; 2868863; -.
DR   KEGG; ani:AN8515.2; -.
DR   KEGG; ani:AN8518.2; -.
DR   VEuPathDB; FungiDB:AN8518; -.
DR   eggNOG; ENOG502SIN0; Eukaryota.
DR   OMA; VQYVHIG; -.
DR   OrthoDB; 1189531at2759; -.
DR   BioCyc; MetaCyc:MON-18729; -.
DR   Proteomes; UP000000560; Chromosome V.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IDA:AspGD.
DR   GO; GO:1900796; P:terrequinone A biosynthetic process; IEP:GO_Central.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..355
FT                   /note="Probable NADPH-dependent quinone reductase tdiC"
FT                   /id="PRO_0000436366"
SQ   SEQUENCE   355 AA;  37620 MW;  A37DC0625A45FDB0 CRC64;
     MHAALVPTWS SPCPIYTEIP DPGPPPPEQL QLKVLAVGIP RVVRLRARGI HPTAKSASLP
     YDPSIDGVGI DEQTGIMYYI LPLSASCLAE KVNVDRDNLV PLQPGAPKPQ PRNGPENGYG
     IALGDAADHR AETLDPIAIA GLVNPVSSSW MALRTRVDGE ITGKTVLVLG ATSKSGRAAV
     LVARFLGANK VIGVARREEG LRSVEGLDGW VTSGDMLPGE TGVRFALPDW VGPVHIVLDY
     VGGSVAAGVL GSAEIEEGRE LQYVQVGNLA LELGTGEKHM FETLPGHLIS RKPICIRGSG
     MGSFSRRDLV REMPGLVAFL ARMKAPFGIA SAPMCEVASV WQDEDTKGSR VVIVP