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Database: UniProt
Entry: P32452
LinkDB: P32452
Original site: P32452 
ID   PHA2_YEAST              Reviewed;         334 AA.
AC   P32452; D6W0M9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Probable prephenate dehydratase {ECO:0000305};
DE            Short=PDT;
DE            EC=4.2.1.51 {ECO:0000305|PubMed:1532796, ECO:0000305|PubMed:6060189};
DE   AltName: Full=Phenylalanine-requiring protein 2;
GN   Name=PHA2; OrderedLocusNames=YNL316C; ORFNames=N0351;
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].
RC   STRAIN=S288c / FY1676;
RX   PubMed=7502583; DOI=10.1002/yea.320111109;
RA   Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT   "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
RT   identifies six known genes, a new member of the hexose transporter family
RT   and ten new open reading frames.";
RL   Yeast 11:1077-1085(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=1532796; DOI=10.1016/s0021-9258(18)42529-x;
RA   Ackerman S.H., Martin J., Tzagoloff A.;
RT   "Characterization of ATP11 and detection of the encoded protein in
RT   mitochondria of Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 267:7386-7394(1992).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=6060189; DOI=10.1111/j.1432-1033.1967.tb00083.x;
RA   Lingens F., Goebel W., Uesseler H.;
RT   "Regulation der Biosynthese der aromatischen Aminosaeuren in Saccharomyces
RT   cerevisiae.";
RL   Eur. J. Biochem. 1:363-374(1967).
RN   [6]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
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   -!- FUNCTION: Catayzes the decarboxylation/dehydration of prephenate to
CC       phenylpyruvate. {ECO:0000305|PubMed:1532796,
CC       ECO:0000305|PubMed:6060189}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC         Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC         Evidence={ECO:0000305|PubMed:1532796, ECO:0000305|PubMed:6060189};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21649;
CC         Evidence={ECO:0000305|PubMed:1532796, ECO:0000305|PubMed:6060189};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1. {ECO:0000305|PubMed:1532796}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: By L-phenylalanine. {ECO:0000269|PubMed:6060189}.
CC   -!- MISCELLANEOUS: Present with 2020 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA34448.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA86380.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA96246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z46259; CAA86380.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z71592; CAA96246.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M87006; AAA34448.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006947; DAA10245.1; -; Genomic_DNA.
DR   PIR; S59565; S59565.
DR   RefSeq; NP_014083.2; NM_001183154.1.
DR   AlphaFoldDB; P32452; -.
DR   SMR; P32452; -.
DR   BioGRID; 35523; 61.
DR   DIP; DIP-4269N; -.
DR   IntAct; P32452; 2.
DR   STRING; 4932.YNL316C; -.
DR   MaxQB; P32452; -.
DR   PaxDb; P32452; -.
DR   PRIDE; P32452; -.
DR   EnsemblFungi; YNL316C_mRNA; YNL316C; YNL316C.
DR   GeneID; 855400; -.
DR   KEGG; sce:YNL316C; -.
DR   SGD; S000005260; PHA2.
DR   VEuPathDB; FungiDB:YNL316C; -.
DR   eggNOG; KOG2797; Eukaryota.
DR   HOGENOM; CLU_035008_5_1_1; -.
DR   InParanoid; P32452; -.
DR   OMA; PLMIYRE; -.
DR   BioCyc; YEAST:MON3O-279; -.
DR   UniPathway; UPA00121; UER00345.
DR   PRO; PR:P32452; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P32452; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IMP:SGD.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IMP:SGD.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW   Lyase; Phenylalanine biosynthesis; Reference proteome.
FT   CHAIN           1..334
FT                   /note="Probable prephenate dehydratase"
FT                   /id="PRO_0000119206"
FT   DOMAIN          7..224
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          244..322
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   334 AA;  38225 MW;  1917F12AE5ECC249 CRC64;
     MASKTLRVLF LGPKGTYSHQ AALQQFQSTS DVEYLPAASI PQCFNQLEND TSIDYSVVPL
     ENSTNGQVVF SYDLLRDRMI KKALSLPAPA DTNRITPDIE VIAEQYVPIT HCLISPIQLP
     NGIASLGNFE EVIIHSHPQV WGQVECYLRS MAEKFPQVTF IRLDCSSTSE SVNQCIRSST
     ADCDNILHLA IASETAAQLH KAYIIEHSIN DKLGNTTRFL VLKRRENAGD NEVEDTGLLR
     VNLLTFTTRQ DDPGSLVDVL NILKIHSLNM CSINSRPFHL DEHDRNWRYL FFIEYYTEKN
     TPKNKEKFYE DISDKSKQWC LWGTFPRNER YYHK
//
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