Reviewed, UniProtKB/Swiss-Prot P80647 (DLDH_HYMDI)

Names and origin

Protein names	Recommended name:     Dihydrolipoyl dehydrogenase     EC=1.8.1.4 Alternative name(s):     Dihydrolipoamide dehydrogenase
Organism	Hymenolepis diminuta
Taxonomic identifier	6216 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Platyhelminthes › Cestoda › Eucestoda › Cyclophyllidea › Hymenolepididae › Hymenolepis

Protein attributes

Sequence length	53 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 By similarity. This enzyme has lipoamide dehydrogenase activity and NADH -> NAD transhydrogenation activity. Also displays some NADH-ferricyanide reductase and NADPH -> NAD transydrogenation activities. Ref.1 UniProtKB P09622
Catalytic activity	Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. Ref.1
Cofactor	Binds 1 FAD per subunit By similarity. UniProtKB P00390
Enzyme regulation	Lipoamide reduction and the NADH -> NAD reaction are both completely inhibited by copper and cadmium ions. Ref.1
Subunit structure	Homodimer. Ref.1
Subcellular location	Mitochondrion. Ref.1
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: KM=0.09 mM for NADH for the NADH -> NAD reaction Ref.1 KM=0.18 mM for NADH for the lipoamide dehydrogenase reaction KM=0.23 mM for AcPyAD for the NADH -> NAD reaction Ref.1 KM=0.51 mM for lipoamide Ref.1 pH dependence: Optimum pH is 7.5 for NADH -> NAD transhydrogenation, 6.5 for lipoamide reduction, 4.5 for NADPH -> NAD transhydrogenation, and 6.5 for NADH-ferricyanide reduction. Ref.1

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion 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 electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›53	›53	Dihydrolipoyl dehydrogenase		PRO_0000311713
Regions
	Nucleotide binding	35 – 44	10	FAD By similarity UniProtKB P00390
Sites
	Binding site	53	1	FAD By similarity
Amino acid modifications
	Disulfide bond	44 ↔ 49		Redox-active By similarity UniProtKB P00390
Experimental info
	Non-terminal residue	53	1

Sequences

	Sequence		Length	Mass (Da)
	P80647-1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: D7C11AE8F2F03D94	FASTA	53	5,315
	10 20 30 40 50 LSSGEKDLVV IGSGPGGYVA AIKAAQLGML TVCIEKYPTF GGTCLNVGCI PSK

References

[1]

"Hymenolepis diminuta: mitochondrial NADH --> NAD transhydrogenation and the lipoamide dehydrogenase system." Walker D.J., Burkhart W., Fioravanti C.F. Exp. Parasitol. 85:158-167(1997) [PubMed: 9030666] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION. Tissue: Larva.

Cross-references

3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 96396.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_HYMDI

Accession

Primary (citable) accession number: P80647

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	November 13, 2007
Last modified:	October 13, 2009
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)