ID   DHQA_EMENI              Reviewed;         329 AA.
AC   P25415; C8VTB0; Q5BE93;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 3.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Quinate dehydrogenase;
DE            EC=1.1.1.24;
GN   Name=qutB; ORFNames=AN1137;
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 [GENOMIC DNA].
RX   PubMed=2976880; DOI=10.1007/bf00337715;
RA   Hawkins A.R., Lamb H.K., Smith M., Keyte J.W., Roberts C.F.;
RT   "Molecular organisation of the quinic acid utilization (QUT) gene cluster
RT   in Aspergillus nidulans.";
RL   Mol. Gen. Genet. 214:224-231(1988).
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH;
CC         Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.24;
CC   -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC       biosynthesis; 3-dehydroquinate from D-quinate (NAD(+) route): step 1/1.
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DR   EMBL; X13525; CAA31880.1; -; Genomic_DNA.
DR   EMBL; AACD01000016; EAA66255.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF88071.1; -; Genomic_DNA.
DR   PIR; S08499; S08499.
DR   RefSeq; XP_658741.1; XM_653649.1.
DR   AlphaFoldDB; P25415; -.
DR   SMR; P25415; -.
DR   STRING; 162425.CADANIAP00001492; -.
DR   EnsemblFungi; CBF88071; CBF88071; ANIA_01137.
DR   EnsemblFungi; EAA66255; EAA66255; AN1137.2.
DR   GeneID; 2876912; -.
DR   KEGG; ani:AN1137.2; -.
DR   VEuPathDB; FungiDB:AN1137; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_044063_1_0_1; -.
DR   InParanoid; P25415; -.
DR   OMA; AIYVMRR; -.
DR   OrthoDB; 1033647at2759; -.
DR   BioCyc; MetaCyc:MON-15333; -.
DR   UniPathway; UPA00088; UER00176.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity; IDA:AspGD.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IDA:AspGD.
DR   GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019631; P:quinate catabolic process; IDA:AspGD.
DR   GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   PANTHER; PTHR21089; PTHR21089; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
PE   4: Predicted;
KW   NAD; Oxidoreductase; Quinate metabolism; Reference proteome.
FT   CHAIN           1..329
FT                   /note="Quinate dehydrogenase"
FT                   /id="PRO_0000079892"
FT   CONFLICT        22
FT                   /note="R -> P (in Ref. 1; EAA66255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="V -> L (in Ref. 1; EAA66255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="L -> V (in Ref. 1; EAA66255)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   329 AA;  36090 MW;  468ABB6CBA7E5B57 CRC64;
     MEPITIPTDR DGVAYLYGHP LRNSLSPPLH QTVYNALGLN WTQIPLSTAT GTSFTRSPEI
     STFLSSVRSN PKFVGSSVTM PWKVAIMPHL DDLTEDARQA GACNTIYLRK EDDGKTQYVG
     TNTDCIGIRE ALLQGSPNGA EHFKGKPALI VGGGGTARTA IYVLRKWLGV SKIYIVNRDA
     KEVEAILAED KQRNPSPQVA LVPVSDPSAA ATLEAPVAVV SGIPNYPPQT EEEIRARETL
     RVFLNRQTHE KDQGVILEMC YHPLPWTDIA QIAQDARWKV ILGSEALIWQ GLEQARLWTG
     KDVVSEPGLV EKVQAFVAQT IAERSKSNL