Reviewed, UniProtKB/Swiss-Prot O05940 (DLDH_RHIET)

Names and origin

Protein names	Recommended name:     Probable dihydrolipoyl dehydrogenase     EC=1.8.1.4 Alternative name(s):     Dihydrolipoamide dehydrogenase     E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes     ORF-E3
Organism	Rhizobium etli
Taxonomic identifier	29449 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium

Protein attributes

Sequence length	277 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes 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 By similarity.
Subcellular location	Cytoplasm Potential.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm 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 – 277	›277	Probable dihydrolipoyl dehydrogenase		PRO_0000068041
Regions
	Nucleotide binding	83 – 86	4	NAD By similarity
Sites
	Active site	259	1	Proton acceptor By similarity
	Binding site	17	1	NAD By similarity
	Binding site	51	1	NAD; via amide nitrogen By similarity
	Binding site	125	1	FAD By similarity
	Binding site	133	1	FAD; via amide nitrogen By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	O05940-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: CD3E3B5DB1FE4C4F	FASTA	277	29,547
	10 20 30 40 50 60 EFASFYRSMG VDVTVVEVMP TIMPVEDAEI TAIARKQLEK RGLKIFTSAK VTKVEKGAGS 70 80 90 100 110 120 ITAHVETSDG KVQQITADRM ISAVGVQGNI ENLGLEALGV LTDRRWLVAD GYGKTNVAGI 130 140 150 160 170 180 YAIGDVAGPP IVAHKAEHEG VVCVEKIAGV PNVHPTDKGK VPGCTYCNPQ VASVGLTEAK 190 200 210 220 230 240 AKELGSDIRV GRFSFAANRK AIALGEDQGM VKVIFDKKTG ELLGAHMVGA EVTELIQGFV 250 260 270 VAMNLETTEE ELMHTIFPHP TVSETMKEAV LDAYGRV

References

[1]	"Cloning and transcriptional analysis of the lipA (lipoic acid synthetase) gene from Rhizobium etli." Tate R., Riccio A., Iaccarino M., Patriarca E.J. FEMS Microbiol. Lett. 149:165-172(1997) [PubMed: 9141657] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CE3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11708 Genomic DNA. Translation: CAA72399.1.
3D structure databases
SMR	O05940. Positions 1-276.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 1020.
Family and domain databases
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHER	PTHR22912:SF20. Lipoamide_DH. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PROSITE	PS00076. PYRIDINE_REDOX_1. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_RHIET

Accession

Primary (citable) accession number: O05940

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 1, 1997
Last modified:	February 9, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)