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.
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
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
SMR	P80647. Positions 5-53.
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:	February 9, 2010
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)