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Reviewed, UniProtKB/Swiss-Prot P81420 (ODP3_SOLTU)

Last modified January 20, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesRecommended name:
    55 kDa dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
    EC=2.3.1.12
Alternative name(s):
    E2
    55 kDa dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Subunit structure

Forms a 60-polypeptide structural core By similarity.

Subcellular location

Mitochondrion matrix.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: EC

lipoic acid binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›15›1555 kDa dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162300

Experimental info

Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P81420-1 [UniParc].

Last modified July 15, 1999. Version 1.
Checksum: EA28B063799BE825

FASTA151,449
        10 
SSADSLPXHG AGXMP 

« Hide

References

[1]"Plant mitochondrial pyruvate dehydrogenase complex: purification and identification of catalytic components in potato."
Millar A.H., Knorpp C., Leaver C.J., Hill S.A.
Biochem. J. 334:571-576(1998) [PubMed: 9729464] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: cv. Romano.
Tissue: Tuber.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.12. 296.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameODP3_SOLTU
AccessionPrimary (citable) accession number: P81420
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: January 20, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information