ID   QUTR_EMENI              Reviewed;         901 AA.
AC   Q00784; C8VTB5; Q04133; Q5BE98;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Quinate repressor protein;
GN   Name=qutR; ORFNames=AN1132;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1544567; DOI=10.1016/0378-1119(92)90452-u;
RA   Hawkins A.R., Lamb H.K., Roberts C.F.;
RT   "Structure of the Aspergillus nidulans qut repressor-encoding gene:
RT   implications for the regulation of transcription initiation.";
RL   Gene 110:109-114(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RA   Geever R.F.;
RL   Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [5]
RP   FUNCTION, AND DOMAINS.
RX   PubMed=8294040; DOI=10.1016/0378-1119(93)90446-a;
RA   Hawkins A.R., Lamb H.K., Moore J.D., Roberts C.F.;
RT   "Genesis of eukaryotic transcriptional activator and repressor proteins by
RT   splitting a multidomain anabolic enzyme.";
RL   Gene 136:49-54(1993).
RN   [6]
RP   INTERACTION WITH QUTA.
RX   PubMed=8704987; DOI=10.1099/13500872-142-6-1477;
RA   Lamb H.K., Newton G.H., Levett L.J., Cairns E., Roberts C.F., Hawkins A.R.;
RT   "The QUTA activator and QUTR repressor proteins of Aspergillus nidulans
RT   interact to regulate transcription of the quinate utilization pathway
RT   genese.";
RL   Microbiology 142:1477-1490(1996).
RN   [7]
RP   FUNCTION, AND DOMAINS.
RX   PubMed=8611179; DOI=10.1042/bj3130941;
RA   Lamb H.K., Moore J.D., Lakey J.H., Levett L.J., Wheeler K.A., Lago H.,
RA   Coggins J.R., Hawkins A.R.;
RT   "Comparative analysis of the QUTR transcription repressor protein and the
RT   three C-terminal domains of the pentafunctional AROM enzyme.";
RL   Biochem. J. 313:941-950(1996).
RN   [8]
RP   FUNCTION, INTERACTION WITH QUTA, AND DOMAIN.
RX   PubMed=10926843; DOI=10.1042/bj3500189;
RA   Levett L.J., Si-Hoe S.M., Liddle S., Wheeler K., Smith D., Lamb H.K.,
RA   Newton G.H., Coggins J.R., Hawkins A.R.;
RT   "Identification of domains responsible for signal recognition and
RT   transduction within the QUTR transcription repressor protein.";
RL   Biochem. J. 350:189-197(2000).
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       {ECO:0000269|PubMed:10926843, ECO:0000269|PubMed:8294040,
CC       ECO:0000269|PubMed:8611179}.
CC   -!- SUBUNIT: Interacts with qutA; transcriptional activator of the quinate
CC       utilization pathway genes. {ECO:0000269|PubMed:10926843,
CC       ECO:0000269|PubMed:8704987}.
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. {ECO:0000269|PubMed:10926843,
CC       ECO:0000269|PubMed:8294040, ECO:0000269|PubMed:8611179}.
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   ---------------------------------------------------------------------------
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; M77664; AAC79663.1; -; Genomic_DNA.
DR   EMBL; M59935; AAC61876.1; -; Genomic_DNA.
DR   EMBL; AACD01000016; EAA66250.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF88080.1; -; Genomic_DNA.
DR   PIR; JH0262; JH0262.
DR   RefSeq; XP_658736.1; XM_653644.1.
DR   AlphaFoldDB; Q00784; -.
DR   SMR; Q00784; -.
DR   STRING; 162425.CADANIAP00001497; -.
DR   EnsemblFungi; CBF88080; CBF88080; ANIA_01132.
DR   EnsemblFungi; EAA66250; EAA66250; AN1132.2.
DR   GeneID; 2876909; -.
DR   KEGG; ani:AN1132.2; -.
DR   VEuPathDB; FungiDB:AN1132; -.
DR   eggNOG; KOG0692; Eukaryota.
DR   HOGENOM; CLU_008871_0_1_1; -.
DR   InParanoid; Q00784; -.
DR   OMA; MIVSCIP; -.
DR   OrthoDB; 187464at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:AspGD.
DR   GO; GO:0019631; P:quinate catabolic process; IMP:AspGD.
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   1: Evidence at protein level;
KW   Quinate metabolism; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..901
FT                   /note="Quinate repressor protein"
FT                   /id="PRO_0000402436"
FT   REGION          1..88
FT                   /note="Sufficient for repression"
FT   REGION          26..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   901 AA;  100343 MW;  02306409F0DDF228 CRC64;
     MSILVRPPKR RLADTENLDQ NHRRVLRDFG QGNSASTPIN TSADYGRFDE RPGSGDGSRY
     ASPFQELSSS QGSLTRVEDS LQTRRKFPPN ASIVLIGIRG TGKSSLAVML AASYGRRVIE
     ADLYFQRVTG RCRGVYKREH TLSEYRRQEA IVMESLLMEH QENCVIVCGP GDVERNGQMR
     LREYAKTHPV IHIVRDLESI QSYLKARDTE KVRRFLELSG PIYRSCSNLE FFNVSEKGIS
     DQPSAKDSQH YTQWDAEVDQ RTQTTTPFLM LKRLQRDFLR FVALATGNIP ELRNQLSPFP
     LHMQPIESRK FTYAATVPIS HLLENDVDIE ELESTADAFE LKIDVSAAPS ARLGTESNLA
     DSISHTVATV RRNIIVPMIY HVESSVFPDS APLRRSDASY LELVLHGLRL GPEFVTVDLS
     FEDSILSQII GTKGSSKVIG HYSQTQPPPQ GWSDPEYEAI YERAKKLGCD MVRLTQPATT
     IDDNFAVERF RHQIKTLPGP QLPVIAYNSG PLGRQSCCFN PVLTPVIPRS LISQSGTKGL
     PSITIQEAQE ALYSSFVLDP MQFFVFGANT TYSLSPAMHN AAFKVRGMPH IYRIHQSPTL
     RGINYLVENP NFGGTSVSLP YKTEVIPLLH SMSPHARAIG AVNTLIPIRN LEGSTDNALD
     LEKNRAGPIK GLHGDNTDWI GIGICIRRGL SPANAIRPST TGLIIGAGGM ARAGIYAMIH
     LGVQNIFIWN RTVANAEKLA QHYMRLNLCT LGGSGSASYT IHVLKSLQES WPANYKQPTI
     VVSGIPAHRI GDQPAPNFQL PPQWIESPTG GVVVDLAYKP LNTPLMRQIR SLSHRGWAAL
     DGLDVLPEQG FAQFELFTGC RAPRRLMRTV ILQEYKEEEQ GEEYDQSAMR TRLENLDGQP
     M