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P12695 (ODP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 147. 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:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name=PDC-E2
Short name=PDCE2
Gene names
Name:LAT1
Synonyms:ODP2, PDA2
Ordered Locus Names:YNL071W
ORF Names:N2374
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. Ref.6

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently.

Subunit structure

Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds. Ref.6

Subcellular location

Mitochondrion matrix Ref.7.

Miscellaneous

The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.

Present with 5440 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Ref.1
Chain29 – 482454Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
PRO_0000020483

Regions

Domain35 – 10975Lipoyl-binding

Sites

Active site4551 Potential
Active site4591 Potential

Amino acid modifications

Modified residue751N6-lipoyllysine

Sequences

Sequence LengthMass (Da)Tools
P12695 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 49D64C738926E784

FASTA48251,818
        10         20         30         40         50         60 
MSAFVRVVPR ISRSSVLTRS LRLQLRCYAS YPEHTIIGMP ALSPTMTQGN LAAWTKKEGD 

        70         80         90        100        110        120 
QLSPGEVIAE IETDKAQMDF EFQEDGYLAK ILVPEGTKDI PVNKPIAVYV EDKADVPAFK 

       130        140        150        160        170        180 
DFKLEDSGSD SKTSTKAQPA EPQAEKKQEA PAEETKTSAP EAKKSDVAAP QGRIFASPLA 

       190        200        210        220        230        240 
KTIALEKGIS LKDVHGTGPR GRITKADIES YLEKSSKQSS QTSGAAAATP AAATSSTTAG 

       250        260        270        280        290        300 
SAPSPSSTAS YEDVPISTMR SIIGERLLQS TQGIPSYIVS SKISISKLLK LRQSLNATAN 

       310        320        330        340        350        360 
DKYKLSINDL LVKAITVAAK RVPDANAYWL PNENVIRKFK NVDVSVAVAT PTGLLTPIVK 

       370        380        390        400        410        420 
NCEAKGLSQI SNEIKELVKR ARINKLAPEE FQGGTICISN MGMNNAVNMF TSIINPPQST 

       430        440        450        460        470        480 
ILAIATVERV AVEDAAAENG FSFDNQVTIT GTFDHRTIDG AKGAEFMKEL KTVIENPLEM 


LL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae."
Niu X.-D., Browning K.S., Behal R.H., Reed L.J.
Proc. Natl. Acad. Sci. U.S.A. 85:7546-7550(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-43 AND 148-167.
[2]"Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs."
Poehlmann R., Philippsen P.
Yeast 12:391-402(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"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. expand/collapse author list , 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.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Pyruvate dehydrogenase complex from baker's yeast. 2. Molecular structure, dissociation, and implications for the origin of mitochondria."
Kresze G.B., Ronft H.
Eur. J. Biochem. 119:581-587(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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].
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04096 Genomic DNA. Translation: AAA34385.1.
X86470 Genomic DNA. Translation: CAA60189.1.
Z71347 Genomic DNA. Translation: CAA95945.1.
AY693185 Genomic DNA. Translation: AAT93204.1.
BK006947 Genomic DNA. Translation: DAA10474.1.
PIRA30198.
RefSeqNP_014328.3. NM_001182909.3.

3D structure databases

ProteinModelPortalP12695.
SMRP12695. Positions 39-115, 175-216, 240-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35752. 157 interactions.
DIPDIP-6782N.
IntActP12695. 22 interactions.
MINTMINT-650239.
STRING4932.YNL071W.

Proteomic databases

PaxDbP12695.
PeptideAtlasP12695.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL071W; YNL071W; YNL071W.
GeneID855653.
KEGGsce:YNL071W.

Organism-specific databases

CYGDYNL071w.
SGDS000005015. LAT1.

Phylogenomic databases

eggNOGCOG0508.
GeneTreeENSGT00740000115591.
HOGENOMHOG000281566.
KOK00627.
OMAKSTRISV.
OrthoDBEOG7TTQJ2.

Enzyme and pathway databases

BioCycYEAST:YNL071W-MONOMER.

Gene expression databases

GenevestigatorP12695.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR027189. LAT1_fungal.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERPTHR23151:SF24. PTHR23151:SF24. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979905.
PROP12695.

Entry information

Entry nameODP2_YEAST
AccessionPrimary (citable) accession number: P12695
Secondary accession number(s): D6W1A8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: March 19, 2014
This is version 147 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 XIV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families