ID   QUTR_NEUTR              Reviewed;         917 AA.
AC   Q4U3U3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Quinate repressor protein;
GN   Name=qa-1s;
OS   Neurospora terricola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=88718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Arnett D.R., Asch D.K.;
RT   "Sequence analysis of genes of the quinic acid (qa) cluster of two
RT   homothallic Neurospora species.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; DQ015973; AAY41164.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4U3U3; -.
DR   SMR; Q4U3U3; -.
DR   GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
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   Quinate metabolism; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..917
FT                   /note="Quinate repressor protein"
FT                   /id="PRO_0000260166"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   917 AA;  100522 MW;  8B8103258E3C80FD CRC64;
     MNTIPTRHFG DIAPRDPLSL PPISSSVASG MKRSFTTMAM LYANDSDTGN SDDANARRPP
     RPLSNSPSTS NYRVGSWSAP NSPPRRALPH HPTTANYDPD ASIVIAGIRG AGKSTLAIMA
     STAMKRKIVD LESEFHHLTG LSSSNYKKRH GLADYGRRHI TILQNILNLH RTRAILVCSW
     LERDVQAMLQ DFSTSNPVIY VLRDAKAIEA HLKGYDKSKV GALLDATSAV LRRCTRFEFF
     NVSEENLDTH SGSASPPAVP DQRHTAPYLT LKRAERHFLK FLSLILPKGT IPFVESAFPL
     ASVPVEQRRF TYALALPISA FLDKGVDIQE FDAGVDAIEI IVDDLATSES GPTSPLGLAP
     HRASEISRVV GEIRRDTVIP IILHVVFPER ALYEEALLAL YMAYLSHALR LAPDYLTVDL
     RLDSGLLGQL TAVKGITKAI GNKQLAQVNS PLWGDPSWLQ AYQKAQNTGC DLVRLTRPAS
     GSGDNTDIRQ LQVAVEAAGG PRLPLIAYNT GRLGRTSMCF NEILTPVTPE PFKEDTLGLQ
     NSAHRHLQPP LTALEATQAL YSAFVHDPMK LYVFGANVGY SLSPAMHNAA LKACGISHHY
     RPLSTTNIGT LREVISDPQF AGASVGLPFK VEIISLTHSL SRHAKAIGAV NTLIPVRHLT
     ADGGIPDEVS MFNNISQAGP VKALYGENTD WIGIRACLRR GLSPANAVRS TSTGLVIGAG
     GMARAAVYAM LQLGVKKILI FNRTFANAEK LVLHFENLLA RDALPLLSTG PRSDDNTCFH
     IIRSRDEPLP ENFKNPTMIV SCIPTHTVDN TPDPEFTVPL HWLDNPTGGI VLELDYKCLT
     SPLLEQTRRE AHRGWVAMDG LDLLPEQGFA QFELFTGRRA PRRLMRREVL RAYPDDQEQS
     HTAQLQPRLN KIATQIS