Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Putative prephenate dehydratase

Gene

PHA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Prephenate = phenylpyruvate + H2O + CO2.

Pathwayi: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phenylpyruvate from prephenate.
Proteins known to be involved in this subpathway in this organism are:
  1. Putative prephenate dehydratase (PHA2)
This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phenylpyruvate from prephenate, the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

  • amino acid binding Source: InterPro
  • prephenate dehydratase activity Source: SGD

GO - Biological processi

  • L-phenylalanine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-279.
UniPathwayiUPA00121; UER00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative prephenate dehydratase (EC:4.2.1.51)
Short name:
PDT
Alternative name(s):
Phenylalanine-requiring protein 2
Gene namesi
Name:PHA2
Ordered Locus Names:YNL316C
ORF Names:N0351
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL316C.
SGDiS000005260. PHA2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Putative prephenate dehydratasePRO_0000119206Add
BLAST

Proteomic databases

MaxQBiP32452.

Interactioni

Protein-protein interaction databases

BioGridi35523. 8 interactions.
DIPiDIP-4269N.
IntActiP32452. 2 interactions.
MINTiMINT-503464.

Structurei

3D structure databases

ProteinModelPortaliP32452.
SMRiP32452. Positions 10-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 224218Prephenate dehydratasePROSITE-ProRule annotationAdd
BLAST
Domaini244 – 32279ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation
Contains 1 prephenate dehydratase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000018970.
InParanoidiP32452.
KOiK04518.
OMAiLENSTNG.
OrthoDBiEOG7HQNKD.

Family and domain databases

InterProiIPR002912. ACT_dom.
IPR001086. Preph_deHydtase.
[Graphical view]
PfamiPF00800. PDT. 1 hit.
[Graphical view]
PROSITEiPS51671. ACT. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32452-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKTLRVLF LGPKGTYSHQ AALQQFQSTS DVEYLPAASI PQCFNQLEND
60 70 80 90 100
TSIDYSVVPL ENSTNGQVVF SYDLLRDRMI KKALSLPAPA DTNRITPDIE
110 120 130 140 150
VIAEQYVPIT HCLISPIQLP NGIASLGNFE EVIIHSHPQV WGQVECYLRS
160 170 180 190 200
MAEKFPQVTF IRLDCSSTSE SVNQCIRSST ADCDNILHLA IASETAAQLH
210 220 230 240 250
KAYIIEHSIN DKLGNTTRFL VLKRRENAGD NEVEDTGLLR VNLLTFTTRQ
260 270 280 290 300
DDPGSLVDVL NILKIHSLNM CSINSRPFHL DEHDRNWRYL FFIEYYTEKN
310 320 330
TPKNKEKFYE DISDKSKQWC LWGTFPRNER YYHK
Length:334
Mass (Da):38,225
Last modified:October 17, 2006 - v3
Checksum:i1917F12AE5ECC249
GO

Sequence cautioni

The sequence AAA34448.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA86380.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA96246.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46259 Genomic DNA. Translation: CAA86380.1. Different initiation.
Z71592 Genomic DNA. Translation: CAA96246.1. Different initiation.
M87006 Genomic DNA. Translation: AAA34448.1. Different initiation.
BK006947 Genomic DNA. Translation: DAA10245.1.
PIRiS59565.
RefSeqiNP_014083.2. NM_001183154.1.

Genome annotation databases

EnsemblFungiiYNL316C; YNL316C; YNL316C.
GeneIDi855400.
KEGGisce:YNL316C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46259 Genomic DNA. Translation: CAA86380.1. Different initiation.
Z71592 Genomic DNA. Translation: CAA96246.1. Different initiation.
M87006 Genomic DNA. Translation: AAA34448.1. Different initiation.
BK006947 Genomic DNA. Translation: DAA10245.1.
PIRiS59565.
RefSeqiNP_014083.2. NM_001183154.1.

3D structure databases

ProteinModelPortaliP32452.
SMRiP32452. Positions 10-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35523. 8 interactions.
DIPiDIP-4269N.
IntActiP32452. 2 interactions.
MINTiMINT-503464.

Proteomic databases

MaxQBiP32452.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL316C; YNL316C; YNL316C.
GeneIDi855400.
KEGGisce:YNL316C.

Organism-specific databases

EuPathDBiFungiDB:YNL316C.
SGDiS000005260. PHA2.

Phylogenomic databases

HOGENOMiHOG000018970.
InParanoidiP32452.
KOiK04518.
OMAiLENSTNG.
OrthoDBiEOG7HQNKD.

Enzyme and pathway databases

UniPathwayiUPA00121; UER00345.
BioCyciYEAST:MONOMER3O-279.

Miscellaneous databases

PROiP32452.

Family and domain databases

InterProiIPR002912. ACT_dom.
IPR001086. Preph_deHydtase.
[Graphical view]
PfamiPF00800. PDT. 1 hit.
[Graphical view]
PROSITEiPS51671. ACT. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV identifies six known genes, a new member of the hexose transporter family and ten new open reading frames."
    Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.
    Yeast 11:1077-1085(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / FY1676.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Characterization of ATP11 and detection of the encoded protein in mitochondria of Saccharomyces cerevisiae."
    Ackerman S.H., Martin J., Tzagoloff A.
    J. Biol. Chem. 267:7386-7394(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
  5. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPHA2_YEAST
AccessioniPrimary (citable) accession number: P32452
Secondary accession number(s): D6W0M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 17, 2006
Last modified: July 6, 2016
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2020 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.