Reviewed, UniProtKB/Swiss-Prot P80503 (DLDH_SOLTU)

Names and origin

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

Protein attributes

Sequence length	40 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro 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)
	P80503-1 [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: 8919912] [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: 9729464] [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: 10510296] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20. Strain: cv. Romano. Tissue: Tuber.

Cross-references

3D structure databases
HSSP	HSSP built from PDB template 1LPF based on UniProtKB P14218.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 296.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006258. Lipoamide_DH. IPR012999. Pyr_OxRdtase_I_AS. [Graphical view]
PANTHER	PTHR22912:SF20. Lipoamide_DH. 1 hit.
Pfam	PF07992. Pyr_redox_2. 1 hit. [Graphical view]
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:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)