Q89AQ8 (DLDH_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyl dehydrogenase
EC=1.8.1.4

Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes

Gene names

Name:	lpdA
Ordered Locus Names:	bbp_191

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Baizongia pistaciae)

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
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 By similarity.
Miscellaneous	The active site is a redox-active disulfide bond By similarity.
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
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding 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 – 475	475	Dihydrolipoyl dehydrogenase		PRO_0000068021
Regions
	Nucleotide binding	37 – 46	10	FAD By similarity
	Nucleotide binding	183 – 187	5	NAD By similarity
	Nucleotide binding	272 – 275	4	NAD By similarity
Sites
	Active site	447	1	Proton acceptor By similarity
	Binding site	55	1	FAD By similarity
	Binding site	118	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	206	1	NAD By similarity
	Binding site	239	1	NAD; via amide nitrogen By similarity
	Binding site	315	1	FAD By similarity
	Binding site	323	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	46 ↔ 51		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89AQ8 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A29761D2D44C9BC7	FASTA	475	52,409
	10 20 30 40 50 60 MISKKVDTQV VIIGSGPSGY SAAFRCSDLG LNVVLIEQYY SLGGVCLNVG CIPSKYLLHI 70 80 90 100 110 120 AKVIKDVKKL SRIGISFEKL DINLKEIQCN QKKIIESFSS GISNLARKRN VRIIFGYAKF 130 140 150 160 170 180 LDANSIFVQG EHDSYVVSFN KIVIATGSLS KKLSYIPYDD IRIWNSSFAV SIPSIPKKLL 190 200 210 220 230 240 IIGGGIIGLE MATIYSALGS NVDIIDNSHD ILPHLDRDVI DIFKRSVNHD YNIFFNSNVI 250 260 270 280 290 300 KIVQEKNGLL VHIAENDNKN KRFELYDIIL VAIGRVPNTD MLDISKVGLK TDNNGFIKVN 310 320 330 340 350 360 EQFCTNIPNI YAIGDVIGQP MLAHKGTHEG HIVAEVISGK KHYFNPFVIP CVSYTEPEIA 370 380 390 400 410 420 WVGITENEAR KNNINYEVSS VLWNTLGRAV SSQCSEGVTK LIFDKKTNKI IGGCIVGSNA 430 440 450 460 470 GELLGEISLA IEMGCDAEDL ALTIHAHPTL YESINLSAQI FQGTITDLIN KKIKK

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO26923.1.
RefSeq	NP_777818.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89AQ8.
ModBase	Search...
Protein-protein interaction databases
STRING	224915.bbp191.
Proteomic databases
PRIDE	Q89AQ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO26923; AAO26923; bbp_191.
GeneID	1058236.
KEGG	bab:bbp191.
PATRIC	21245157. VBIBucAph80364_0185.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1249.
KO	K00382.
OMA	FAHKAYA.
Enzyme and pathway databases
BioCyc	BAPH224915:GJ9D-191-MONOMER.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
PANTHER	PTHR22912:SF20. PTHR22912:SF20. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_BUCBP

Accession

Primary (citable) accession number: Q89AQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program