Reviewed, UniProtKB/Swiss-Prot P35484 (DLDH_ACHLA)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of pyruvate complex

Gene names

Name:

pdhD

Organism

Acholeplasma laidlawii

Taxonomic identifier

2148 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	336 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes.
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.
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
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	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 – ›336	›336	Dihydrolipoyl dehydrogenase		PRO_0000068012
Regions
	Nucleotide binding	34 – 42	9	FAD By similarity
	Nucleotide binding	180 – 184	5	NAD By similarity
	Nucleotide binding	264 – 267	4	NAD By similarity
Sites
	Binding site	51	1	FAD By similarity
	Binding site	115	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	203	1	NAD By similarity
	Binding site	237	1	NAD; via amide nitrogen By similarity
	Binding site	304	1	FAD By similarity
	Binding site	312	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	42 ↔ 47		Redox-active By similarity
Experimental info
	Non-terminal residue	336	1

Sequences

	Sequence		Length	Mass (Da)
	P35484-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 4405B1097279B36C	FASTA	336	35,996
	10 20 30 40 50 60 MSKEYEIIIV GGGPGGYVAA IKAAQYGAKV ALVEKEVVGG ICLNHGCIPT KTFLKSAKVF 70 80 90 100 110 120 NTVKKSMDFG VSTSGEVGFD WSKIVSRKDG VVKQLTNGVA FLLKKNGVDV YNGFGDIKSA 130 140 150 160 170 180 NEVVVNGESL KTKNVIIATG SSAVVPPIPG VKEAYEKGIV VTSRELLNVK NYPKSIVIVG 190 200 210 220 230 240 GGVIGVEFAT VFNSFGSKVT IIEMMDGILP TMDDDIRVAY AKTLKRDGIE ILTKAEVKKV 250 260 270 280 290 300 DDHKVTYSLD GKETTIEGDL ILMSVGTRAN SKGLEHLGLE MDRANIKTNE YLQTNVPGVY 310 320 330 AIGDVNGKFM LAHVAEHEGI TAVQHILKIG HAKMNY

References

[1]	"Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii." Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A. J. Bacteriol. 174:1388-1396(1992) [PubMed: 1735725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M81753 Genomic DNA. Translation: AAA21910.1.
PIR	D42653.
3D structure databases
SMR	P35484. Positions 5-335.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 96506.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR006258. Lipoamide_DH. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
PANTHER	PTHR22912:SF20. Lipoamide_DH. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_ACHLA

Accession

Primary (citable) accession number: P35484

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	February 9, 2010
This is version 76 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)