ID   QUTR_TALSN              Reviewed;         820 AA.
AC   P0CI62; B8MQX8;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Quinate repressor protein;
GN   Name=qutR; ORFNames=TSTA_053310.1;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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 qutA activator protein
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with qutA; transcriptional activator of the quinate
CC       utilization pathway genes.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED12813.1; Type=Erroneous gene model prediction; Note=The predicted gene TSTA_053310 has been split into 2 genes: TSTA_053310.1 and TSTA_053310.2.; Evidence={ECO:0000305};
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DR   EMBL; EQ962659; EED12813.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002486924.1; XM_002486879.1.
DR   AlphaFoldDB; P0CI62; -.
DR   SMR; P0CI62; -.
DR   STRING; 28564.XP_002486924.1; -.
DR   EnsemblFungi; EED12813; EED12813; TSTA_053310.
DR   GeneID; 8098282; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_008871_0_1_1; -.
DR   InParanoid; P0CI62; -.
DR   OrthoDB; 187464at2759; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
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; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..820
FT                   /note="Quinate repressor protein"
FT                   /id="PRO_0000402437"
FT   REGION          25..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   820 AA;  91787 MW;  B4A9AA4B38163BA3 CRC64;
     MDTASIRGLS WSTLDPASYN SRKRSFEQML LQQDSNESSR RTSPSRTHSR VDLERHSSHI
     VSLSSSNGSP SLEDPENRLY ESPASARQYY GDESLILVGF PSAGKKTLGL IASAALRREF
     VDFDTVFVGK TGLSPREYIE AHGATAYRSV EDELTSEVFR SRQKGCVLVG FFAMASNRQR
     RLLKSLSTTN PIIHIQRDLG NMIHRGDSDK DRLYRTYQLS EKMHRRFANF EFFNIFQPMA
     DDKPLGPLRL KATEREFVRF LNGIFPQSEA SRGLKNLCSS SYTYALQAPS SWLDDPQADY
     TELDSGADAV EILVEMSPQN QQDLFFKLSQ RVAVLRKYCR VPIILDLETS ATMNYIAQVN
     LLELVIRQAP DVIMVSLDMS PHLVKQLSLA KGHSKIIGKY HQKGPISENW DLTNLQTVID
     KASLLHCSAI RLTGEAYETN NNFGCVRVVL EARKLSDLPV SCYNTGEYGR SSICLNPILS
     PVVLPSQSTK QGITLADAQR GLFSSFWRTK KNFTVFGQNV SYSLTPAMHN AACIACGMPH
     TCDYVESDRL ARIREVFERE SQGGLAIVYP YKTEVVQMMD EMSLDAKVIG AVNTVVIERI
     STNEGSPKLY LKGYNTDHIG IRTCIEKNLS PANAIRSQTS ALIIGAGGMA RAAIYACIKA
     GVRNICIFNR TEANARRLAD YFATVYTNLR LTILTDLSTP WPTDLWHPTI IVSCIPAHKV
     GDNDAPDFLI PEQWLGSSTG GVFVEFAYKP LVTRLIRFMQ SRRSQGWIVA DGLDVLVEQG
     IAQFEILTDR PAPSHIMRRT VREQYSIAQN AHSDHETTET