P80503 (DLDH_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Dihydrolipoyl dehydrogenase EC=1.8.1.4 Alternative name(s): Dihydrolipoamide dehydrogenase
Organism	Solanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier	4113 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	40 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. The pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion matrix.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›40	›40	Dihydrolipoyl dehydrogenase		PRO_0000068010
Regions
	Nucleotide binding	36 – 40	5	FAD By similarity
Experimental info
	Non-terminal residue	40	1

Sequences

	Sequence		Length	Mass (Da)
	P80503 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 17397BE30C2E9523	FASTA	40	3,913
	10 20 30 40 ASGSDENDVV VIGGGPGGYV AAIKAAQLGL KTTXIEKRGT

References

[1]	"New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria." Jansch L., Kruft V., Schmitz U.K., Braun H.P. Plant J. 9:357-368(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Tuber.
[2]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20. Strain: cv. Romano. Tissue: Tuber.
[3]	"Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and characterization in potato." Millar A.H., Hill S.A., Leaver C.J. Biochem. J. 343:327-334(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20. Strain: cv. Romano. Tissue: Tuber.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
PROSITE	PS00076. PYRIDINE_REDOX_1. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_SOLTU

Accession

Primary (citable) accession number: P80503

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program