Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P12695 (ODP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 139. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Lipoyl Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay PubMed 7947791. Source: SGD
Cellular_component	mitochondrial pyruvate dehydrogenase complex Inferred from direct assay PubMed 2007123 PubMed 9038189. Source: SGD
Molecular_function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from direct assay PubMed 2271545. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

Mitochondrion Ref.1

Chain

29 – 482

454

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

PRO_0000020483

Regions

Domain

35 – 109

Lipoyl-binding

Sites

Active site

455

Potential

Active site

459

Potential

Amino acid modifications

Modified residue

N6-lipoyllysine

Modified residue

280

Phosphoserine Ref.9

Modified residue

281

Phosphoserine Ref.9

Sequences

Sequence

Length

Mass (Da)

Tools

P12695 [UniParc].

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

482

51,818

        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

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References

	« Hide 'large scale' referencesShow '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. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-281, MASS SPECTROMETRY.
+	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.
PIR	A30198.
RefSeq	NP_014328.3. NM_001182909.3.
3D structure databases
ProteinModelPortal	P12695.
SMR	P12695. Positions 39-115, 173-212, 240-482.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6782N.
IntAct	P12695. 20 interactions.
MINT	MINT-650239.
STRING	4932.YNL071W.
Proteomic databases
PaxDb	P12695.
PeptideAtlas	P12695.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL071W; YNL071W; YNL071W.
GeneID	855653.
KEGG	sce:YNL065W. sce:YNL071W.
Organism-specific databases
CYGD	YNL071w.
SGD	S000005015. LAT1.
Phylogenomic databases
eggNOG	COG0508.
GeneTree	ENSGT00560000077144.
HOGENOM	HOG000281566.
KO	K00627.
OMA	GTICISN.
OrthoDB	EOG4CC78S.
Gene expression databases
Genevestigator	P12695.
GermOnline	YNL071W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	IPR003016. 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]
PANTHER	PTHR23151:SF24. PTHR23151:SF24. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979905.

Entry information

Entry name

ODP2_YEAST

Accession

Primary (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:	May 1, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIV

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents