ID   DHQA_NEUCR              Reviewed;         339 AA.
AC   P11635; Q7RVA1;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Quinate dehydrogenase;
DE            EC=1.1.1.24;
GN   Name=qa-3; ORFNames=NCU06025;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=2525625; DOI=10.1016/0022-2836(89)90438-5;
RA   Geever R.F., Huiet L., Baum J.A., Tyler B.M., Patel V.B., Rutledge B.J.,
RA   Case M.E., Giles N.H.;
RT   "DNA sequence, organization and regulation of the qa gene cluster of
RT   Neurospora crassa.";
RL   J. Mol. Biol. 207:15-34(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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.
CC   -!- INDUCTION: By quinic acid and the positive regulator qa-1f.
CC   -!- MISCELLANEOUS: N.crassa can utilize quinic acid as sole carbon source,
CC       oxidizing it to protocatechuic acid and ultimately to succinic acid and
CC       acetic acid. The conversion of quinic acid to protocatechuic acid is
CC       catalyzed by enzymes which are encoded by three coordinately regulated
CC       genes comprising the qa gene cluster.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA32751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X14603; CAA32751.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002242; EAA30379.3; -; Genomic_DNA.
DR   PIR; S04253; S04253.
DR   RefSeq; XP_959615.3; XM_954522.3.
DR   AlphaFoldDB; P11635; -.
DR   SMR; P11635; -.
DR   STRING; 5141.EFNCRP00000005363; -.
DR   EnsemblFungi; EAA30379; EAA30379; NCU06025.
DR   GeneID; 3875774; -.
DR   KEGG; ncr:NCU06025; -.
DR   VEuPathDB; FungiDB:NCU06025; -.
DR   HOGENOM; CLU_044063_1_0_1; -.
DR   InParanoid; P11635; -.
DR   UniPathway; UPA00088; UER00176.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IBA:GO_Central.
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:0019630; P:quinate metabolic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Quinate metabolism; Reference proteome.
FT   CHAIN           1..339
FT                   /note="Quinate dehydrogenase"
FT                   /id="PRO_0000079893"
SQ   SEQUENCE   339 AA;  37271 MW;  8A951802A06C03D4 CRC64;
     MSTATTTTSA TTTMSVVQPR QQELLHLTST PDITPYTRHG YLFGQKLAAS MSPLLHSIVY
     SHLSLNWAQL RLDSPSIPLF LQLAQHPDFY GASVTMPHKV AIIPHLDHLT PECRDVGACN
     TLFLKTDPAT GRRLYCGANT DVIGVRESFV QNVSDPARVY ESRPALVIGG GGAARSAVYA
     LHKWLGATDI YLVNRDKSEV DAVIAECTER GYGDRLVHVA SVEQAEGLEG PGAIVACIPD
     FPPKTEKEML VRRIVETFLM KEEKGAMLEM CYNPSPFTEL GALAEHEGWQ VILGTEALIW
     QGIEQDKYWT GRTNEELPIQ QIKEVIAAKL AEASKSHTS