TYR1_YEAST
ID TYR1_YEAST Reviewed; 452 AA.
AC P20049; D6VQG2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Prephenate dehydrogenase [NADP(+)];
DE Short=PRDH;
DE EC=1.3.1.13;
GN Name=TYR1; OrderedLocusNames=YBR166C; ORFNames=YBR1218;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2697638; DOI=10.1016/0378-1119(89)90422-8;
RA Mannhaupt G., Stucka R., Pilz U., Schwarzlose C., Feldmann H.;
RT "Characterization of the prephenate dehydrogenase-encoding gene, TYR1, from
RT Saccharomyces cerevisiae.";
RL Gene 85:303-311(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADPH; Xref=Rhea:RHEA:21640, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.13;
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
CC -!- INDUCTION: Presence of Phe represses the TYR1 gene expression.
CC -!- MISCELLANEOUS: Present with 2180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Z36035; CAA85127.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07282.1; -; Genomic_DNA.
DR PIR; S46037; S46037.
DR RefSeq; NP_009725.1; NM_001178514.1.
DR AlphaFoldDB; P20049; -.
DR SMR; P20049; -.
DR BioGRID; 32866; 112.
DR DIP; DIP-4627N; -.
DR IntAct; P20049; 12.
DR MINT; P20049; -.
DR STRING; 4932.YBR166C; -.
DR iPTMnet; P20049; -.
DR MaxQB; P20049; -.
DR PaxDb; P20049; -.
DR PRIDE; P20049; -.
DR EnsemblFungi; YBR166C_mRNA; YBR166C; YBR166C.
DR GeneID; 852464; -.
DR KEGG; sce:YBR166C; -.
DR SGD; S000000370; TYR1.
DR VEuPathDB; FungiDB:YBR166C; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_1_0_1; -.
DR InParanoid; P20049; -.
DR OMA; WWKLGIV; -.
DR BioCyc; YEAST:YBR166C-MON; -.
DR UniPathway; UPA00122; UER00962.
DR PRO; PR:P20049; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P20049; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IDA:SGD.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IDA:SGD.
DR GO; GO:0006570; P:tyrosine metabolic process; IMP:SGD.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003099; Prephen_DH.
DR InterPro; IPR012385; Prephenate_DH_fun.
DR Pfam; PF02153; PDH; 1.
DR PIRSF; PIRSF036510; PDH_fung; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NADP;
KW Oxidoreductase; Reference proteome; Tyrosine biosynthesis.
FT CHAIN 1..452
FT /note="Prephenate dehydrogenase [NADP(+)]"
FT /id="PRO_0000119208"
FT DOMAIN 14..297
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT BINDING 14..43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT CONFLICT 38
FT /note="G -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 204..211
FT /note="IKIYPWTL -> DKDSSLDS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..313
FT /note="GN -> SD (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..452
FT /note="MIKTILSHSSDRSAAEKRNT -> DDKNHSESF (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50923 MW; D483B93ABBC8F8F4 CRC64;
MVSEDKIEQW KATKVIGIIG LGDMGLLYAN KFTDAGWGVI CCDREEYYDE LKEKYASAKF
ELVKNGHLVS RQSDYIIYSV EASNISKIVA TYGPSSKVGT IVGGQTSCKL PEIEAFEKYL
PKDCDIITVH SLHGPKVNTE GQPLVIINHR SQYPESFEFV NSVMACLKSK QVYLTYEEHD
KITADTQAVT HAAFLSMGSA WAKIKIYPWT LGVNKWYGGL ENVKVNISLR IYSNKWHVYA
GLAITNPSAH QQILQYATSA TELFSLMIDN KEQELTDRLL KAKQFVFGKH TGLLLLDDTI
LEKYSLSKSS IGNSNNCKPV PNSHLSLLAI VDSWFQLGID PYDHMICSTP LFRIFLGVSE
YLFLKPGLLE QTIDAAIHDK SFIKDDLEFV ISAREWSSVV SFANFDIYKK QFQSVQKFFE
PMLPEANLIG NEMIKTILSH SSDRSAAEKR NT
