ID   QUTR_NEUAF              Reviewed;         919 AA.
AC   Q4U3U5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Quinate repressor protein;
GN   Name=qa-1s;
OS   Neurospora africana.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=5143;
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; DQ015972; AAY41162.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4U3U5; -.
DR   SMR; Q4U3U5; -.
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..919
FT                   /note="Quinate repressor protein"
FT                   /id="PRO_0000260165"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   919 AA;  100710 MW;  4A3DA96995F64B3F CRC64;
     MNNIPARHVG DVAARDPLPL PHKSSSVASG MKRSFATMAM LYANDSDTGN SDDAGSNARR
     PPRPLSNSPS TSNYRVGSWS APNSPPRRAL PYYPITASFD ADASIVVAGI RGAGKSTLAI
     MASTAMKRKI VDLESEFHHL TGLSSSTYKK RHGPADYGRR QITILQNILN LHRTRAILVC
     SWLERDVQAL LQDFSTSNPV IYVLRDAKAI EAHLKGYDKS KVGTLLDATS AVLRRCTRFE
     FFNVSEENLD THSGSASPPA VPDQRHTAPY LTLKRAERHF LKFLSLILPK GTIPFVESAF
     PLASVPVEQR RFTYALALSI SAFLDKGVDI QELDAGVDAI EIIVDDLATS ESGPASPLGL
     APHRASDISR VVGEIRRDTV IPIILHVVFP ERALHEEALL VLYMAYLTHA LRLAPDYLTV
     DLRLDSGLLG QLTAVKGITK VIGNKQLADA NSPLWGDPSW LLAYQKAQNT GCDLVRLTRP
     ASNSRDNTDI RQFQVAVEAV GGPRLPFISY NTGRLGRTSM CFNEILTPVT PEPFKEDTLG
     LQNSANRHLQ PPLTALEATQ ALYSAFVHDP MKLYVFGANV GYSLSPAMHN AALKACGIPH
     HYRPLSTANI GTLREVISDP QFAGASVGLP FKVEIISLTH SLSRHAKAIG AVNTLIPVRH
     LSADGGIPDE VSMFNNISQA GPVKALYGEN TDWIGIRACL RRGLSPANAV RSTSTGLVIG
     AGGMARAAVY AMLQLGVKKI LIFNRTFANA EKLVLHFENL LARDALPLLS TGPRSHDNTS
     FHIIRSRDEL LPENFKNPTM IVSCIPTHTV DNTPDPEFTV PLHWLDNPTG GIVLELDYKC
     LTSPLLEQTR REAHRGWVAM DGLDLLPEQG FAQFELFTGR RAPRRLMRRE VLRAYPDDQE
     KSYTAQLQPR LNKIATQIS