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Q12511 (PDP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial

Short name=PDP 1
EC=3.1.3.43
Alternative name(s):
Phosphatase two C protein 5
Protein phosphatase 2C homolog 5
Short name=PP2C-5
Protein phosphatase of PDH protein 1
Pyruvate dehydrogenase complex phosphatase 1
Short name=PDC phosphatase 1
Gene names
Name:PTC5
Synonyms:PPP1
Ordered Locus Names:YOR090C
ORF Names:YOR3157C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dephosphorylation and concomitant reactivation of the E1 alpha subunit (PDA1) of the pyruvate dehydrogenase complex. Ref.6 Ref.7

Catalytic activity

[Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate.

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Subcellular location

Mitochondrion intermembrane space Ref.5 Ref.6 Ref.8.

Post-translational modification

Processed by mitochondrial inner membrane protease (IMP) complex and released to the intermembrane space.

Miscellaneous

Present with 7550 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 572[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrialPRO_0000057778

Regions

Domain143 – 572430PP2C-like

Sites

Metal binding1971Manganese 1 By similarity
Metal binding1971Manganese 2 By similarity
Metal binding1981Manganese 1; via carbonyl oxygen By similarity
Metal binding4241Manganese 2 By similarity
Metal binding4801Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12511 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 07A5AF33FA72CC2A

FASTA57263,669
        10         20         30         40         50         60 
MSPLTRTVAI KKTVKVLSKC QSGREYTQKF LQRAYSTSHA NSTYYSRTKL FISSHSKALN 

        70         80         90        100        110        120 
IALLSGSLLL TYSYYSPKKI LSLDTINGIK DYSTNTSGNI NMPSPNPKGT ETQKSQRSQN 

       130        140        150        160        170        180 
DQSVLILNDS KIEAKLHDRE ESHFVNRGTG IFRYDVAQLP SNHPIEDDHV EQIITIPIES 

       190        200        210        220        230        240 
EDGKSIEKDL YFFGIFDGHG GPFTSEKLSK DLVRYVAYQL GQVYDQNKTV FHSDPNQLID 

       250        260        270        280        290        300 
SAISKGFLKL DNDLVIESFR KLFQDPNNTN IANTLPAISG SCALLSLYNS TNSILKVAVT 

       310        320        330        340        350        360 
GDSRALICGL DNEGNWTVKS LSTDQTGDNL DEVRRIRKEH PGEPNVIRNG RILGSLQPSR 

       370        380        390        400        410        420 
AFGDYRYKIK EVDGKPLSDL PEVAKLYFRR EPRDFKTPPY VTAEPVITSA KIGENTKFMV 

       430        440        450        460        470        480 
MGSDGLFELL TNEEIASLVI RWMDKNMNLA PVKAEPGKLP KVIDVSEDKE AQRPAFRYKD 

       490        500        510        520        530        540 
NNSSSPSGSN PEYLIEDKNV ATHLIRNALS AGGRKEYVSA LVSIPSPMSR RYRDDLTVTV 

       550        560        570 
AFFGDSGTPS IVSNATSIVM NPEATTKPKP RL 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequencing and analysis of 130 kb from yeast chromosome XV."
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C., Schwager C., Paces V., Sander C., Ansorge W.
Yeast 13:655-672(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[6]"YIL042c and YOR090c encode the kinase and phosphatase of the Saccharomyces cerevisiae pyruvate dehydrogenase complex."
Krause-Buchholz U., Gey U., Wunschmann J., Becker S., Rodel G.
FEBS Lett. 580:2553-2560(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases."
Gey U., Czupalla C., Hoflack B., Rodel G., Krause-Buchholz U.
J. Biol. Chem. 283:9759-9767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Intermembrane space proteome of yeast mitochondria."
Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.
Mol. Cell. Proteomics 11:1840-1852(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, POST-TRANSLATIONAL MODIFICATION, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X94335 Genomic DNA. Translation: CAA64011.1.
Z74998 Genomic DNA. Translation: CAA99287.1.
BK006948 Genomic DNA. Translation: DAA10867.1.
PIRS61650.
RefSeqNP_014733.1. NM_001183509.1.

3D structure databases

ProteinModelPortalQ12511.
SMRQ12511. Positions 149-543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34488. 40 interactions.
DIPDIP-6439N.
IntActQ12511. 6 interactions.
MINTMINT-672855.
STRING4932.YOR090C.

Proteomic databases

PaxDbQ12511.
PeptideAtlasQ12511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR090C; YOR090C; YOR090C.
GeneID854257.
KEGGsce:YOR090C.

Organism-specific databases

CYGDYOR090c.
SGDS000005616. PTC5.

Phylogenomic databases

eggNOGCOG0631.
GeneTreeENSGT00390000006874.
HOGENOMHOG000209682.
KOK01102.
OMAKPEVTYH.
OrthoDBEOG7XWPXK.

Enzyme and pathway databases

BioCycYEAST:G3O-33624-MONOMER.

Gene expression databases

GenevestigatorQ12511.

Family and domain databases

Gene3D3.60.40.10. 2 hits.
InterProIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. SSF81606. 2 hits.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976185.

Entry information

Entry namePDP1_YEAST
AccessionPrimary (citable) accession number: Q12511
Secondary accession number(s): D6W2F1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families