Q8K9T7 (DLDH_BUCAP) 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:	BUsg_201

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	476 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 – 476	476	Dihydrolipoyl dehydrogenase		PRO_0000068020
Regions
	Nucleotide binding	36 – 45	10	FAD By similarity
	Nucleotide binding	182 – 186	5	NAD By similarity
	Nucleotide binding	271 – 274	4	NAD By similarity
Sites
	Active site	446	1	Proton acceptor By similarity
	Binding site	54	1	FAD By similarity
	Binding site	117	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	205	1	NAD By similarity
	Binding site	238	1	NAD; via amide nitrogen By similarity
	Binding site	314	1	FAD By similarity
	Binding site	322	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	45 ↔ 50		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9T7 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 2BCD5F1ECB08BA58	FASTA	476	52,187
	10 20 30 40 50 60 MHQEIQSEVV IIGSGPAGYS AAFRCADLGL ETVLIEHQER LGGVCLNVGC IPSKSLLHIA 70 80 90 100 110 120 KIIKDASELS ESGVFFNKPI IDIKKINNWK EKIIKKLTTG LSNMGEKRKV RIVQGKALFN 130 140 150 160 170 180 TDHSVLVKNK KNDFTIFFKH AIIATGSKPI KIPSLPNEDN RIWNSTDALS LKSIPNRFLI 190 200 210 220 230 240 IGGGIIGLEM ATIYSALGSK VDIVDRFNAF LPSVDKDITD IYIKSIKKRF KLLLNTHVKS 250 260 270 280 290 300 VEKSKDNDLI VKIAEENSDE NVCCYDNILV AIGRSPNVDF LGLEKIGLKL NESGFIEINQ 310 320 330 340 350 360 QLKTNISHIY AIGDVTGFPM LAHKAVQQAH IAAEVISGKK HYFEPKVIPS VAYTDPEIAW 370 380 390 400 410 420 VGLSEKEAEN NDIDYEVSLF PWSASGRAHA SNCTLGMTKL IFNKNTNKII GGSIIGTNAS 430 440 450 460 470 ELISEIGLAI EMGSDAEDIS LTIHPHPTLS ESISLASEVF QGTITDLLNL KKSLLN

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67765.1.
RefSeq	NP_660554.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9T7.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg201.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67765; AAM67765; BUsg_201.
GeneID	1005398.
KEGG	bas:BUsg201.
PATRIC	21247189. VBIBucAph100086_0208.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1249.
KO	K00382.
OMA	KFPWSAS.
ProtClustDB	CLSK315791.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-267-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_BUCAP

Accession

Primary (citable) accession number: Q8K9T7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program