PHA2_YEAST
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
