ID   QUTR_NEUCR              Reviewed;         918 AA.
AC   P11637; Q7RV99;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 3.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=Quinate repressor protein;
GN   Name=qa-1s; ORFNames=NCU06027;
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   -!- FUNCTION: Multi-domain repressor protein that negatively regulates
CC       transcription of the quinate utilization pathway genes. May mediate its
CC       repressor activity by binding directly to the qa-1f activator protein
CC       (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: Is homologous throughout its length with the C-terminal 3
CC       domains of the pentafunctional AROM protein. The function of the 2 C-
CC       terminal domains may be to act as a molecular sensor that detects the
CC       presence of quinate pathway intermediates as a prerequisite for the
CC       presumed conformational changes necessary for the control of
CC       transcription regulation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase
CC       family. {ECO:0000305}.
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DR   EMBL; X14603; CAA32753.1; -; Genomic_DNA.
DR   EMBL; CM002242; EAA30381.2; -; Genomic_DNA.
DR   PIR; S04255; S04255.
DR   RefSeq; XP_959617.2; XM_954524.2.
DR   AlphaFoldDB; P11637; -.
DR   SMR; P11637; -.
DR   STRING; 5141.EFNCRP00000005472; -.
DR   EnsemblFungi; EAA30381; EAA30381; NCU06027.
DR   GeneID; 3875776; -.
DR   KEGG; ncr:NCU06027; -.
DR   VEuPathDB; FungiDB:NCU06027; -.
DR   HOGENOM; CLU_008871_0_1_1; -.
DR   InParanoid; P11637; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00502; DHQase_I; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR001381; DHquinase_I.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041121; SDH_C.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR   Pfam; PF01487; DHquinase_I; 1.
DR   Pfam; PF18317; SDH_C; 1.
DR   Pfam; PF01488; Shikimate_DH; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   Pfam; PF01202; SKI; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Quinate metabolism; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..918
FT                   /note="Quinate repressor protein"
FT                   /id="PRO_0000097133"
FT   REGION          47..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   918 AA;  100580 MW;  67EDA399CBF098B2 CRC64;
     MNTIPARHVG DVAARDPLPL PHISSSVASG MKRSFATMAM LYNDTGNSND VGAHARRPPR
     TLSNSRSTSA HRVPLGSWSA PNSPPRRALP HHPITASFDP DASIVIAGIR GAGKSTLAIM
     ASTAMKRKIV DLESEFHHLT GLSSSSYKKT HGPVDYGRRQ IAILQNILNL HRTRAILVCS
     WLERDVQAML QDFSVSNPVI YVLRDAKAIE AHLKGYDKSK VGTLLDATST VLRRCTRFEF
     FNVSEENLDT HSASTSPPAV PDQRHTAPYL TLKRAERHFL KFLSLILPKG TIPFVESAFP
     LASVPVEQRR FTYALALPVS ALLDKGVDIQ ELDVGVDAIE IIVDDLATSE SGPTSPLGLA
     PHRASEISRV VGEIRRDTVI PIILHVVFPE RALYEEALLA LYMTYLNHAL RLAPDYLTVD
     LGLDSGLLGQ LTTVQGTTKV IGNKQLAEVN SPRWGDPSWL QAYEKAQNTG CDLVRLTRPA
     SNPRDNTDIR QFHVAVEAVG GPRLPFIAYN TGRLGRTSMC FNEILTPVTP VPTKEDAIGL
     RNPAHRYLQP PLTALEATQA LYSAFVHDPM KLYVFGANVG YSLSPAMHNA ALKACGIPHH
     YKPLSTANIG TLREVISDPQ FAGASVGLPF KVEIISLTHS LSRHAKAIGA VNTLIPVRHL
     TADGGIPDEV SMFNNISQAG AVRALYGENT DWIGIRACLR RGLSPANAVR STSTGLVIGA
     GGMARAAVYA MLQLGVKKIL IFNRTFANAE KLVLHFENLL VRDALPLLST GPRSHDNTCF
     HIIRSRDDPL PENFKNPTMI VSCIPTHTVD NTPDPEFTVP LHWLDNPTGG IVLELDYKCL
     TSPLLEQTRR EAHRGWVAMD GLDLLPEQGF AQFELFTGRR APRRLMRREV LRAYPDDQAK
     SHTAQLQPRL NGIATQIS