Reviewed, UniProtKB/Swiss-Prot P31046 (DLDH3_PSEPU)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase 3
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase 3
      Short name=LPD-3

Gene names

Name:

lpd3

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	LPD-3 may substitute for lipoamide dehydrogenase of the 2-oxoglutarate dehydrogenase and pyruvate multienzyme complexes when the latter is inactive or missing.
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.
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
Technical term	Direct protein sequencing
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 – 466	466	Dihydrolipoyl dehydrogenase 3		PRO_0000068040
Regions
	Nucleotide binding	33 – 42	10	FAD By similarity
	Nucleotide binding	181 – 185	5	NAD By similarity
	Nucleotide binding	271 – 274	4	NAD By similarity
Sites
	Active site	445	1	Proton acceptor By similarity
	Binding site	51	1	FAD By similarity
	Binding site	115	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	204	1	NAD By similarity
	Binding site	238	1	NAD; via amide nitrogen By similarity
	Binding site	313	1	FAD By similarity
	Binding site	321	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	42 ↔ 47		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P31046-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: E805AC5E879881F3	FASTA	466	49,257
	10 20 30 40 50 60 MKSYDVVIIG GGPGGYNAAI RAGQLGLTVA CVEGRSTLGG TCLNVGCMPS KALLHASELY 70 80 90 100 110 120 EAASGDEFAH LGIEVKPTLN LAQMMKQKDE SVTGLTKGIE YLFRKNKVDW IKGWGRLDGV 130 140 150 160 170 180 GKVVVKAEDG SETALQAKDI VIATGSEPTP LPGVTIDNQR IIDSTGALSL PQVPKHLVVI 190 200 210 220 230 240 GAGVIGLELG SVWRRLGSQV TVIEYLDRIC PGTDTETAKT LQKALAKQGM VFKLGSKVTQ 250 260 270 280 290 300 ATASADGVSL VLEPAAGGTA ESLQADYVLV AIGRRPYTKG LNLESVGLET DKRGMLAQRT 310 320 330 340 350 360 PPTSVPGVWV IGDVTSGPML AHKAEDEAVA CIERIAGKPH EVNYNLIPGV IYTRPELATV 370 380 390 400 410 420 GKTEEQLKAE GRAYKVGKFP FTANSRAKIN HETEGFAKVI ADAETDEVLG VHLVGPSVSE 430 440 450 460 MIGEFCVAME FSASAEDIAL TCHPHPTRSE ALRQAAMNVD GMAMQI

References

[1]	"Cloning, sequence and transcriptional analysis of the structural gene for LPD-3, the third lipoamide dehydrogenase of Pseudomonas putida." Palmer J.A., Madhusudhan K.T., Hatter K., Sokatch J.R. Eur. J. Biochem. 202:231-240(1991) [PubMed: 1722146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G2.
[2]	"Isolation of a third lipoamide dehydrogenase from Pseudomonas putida." Burns G., Sykes P.J., Hatter K., Sokatch J.R. J. Bacteriol. 171:665-668(1989) [PubMed: 2914869] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X55704 Genomic DNA. Translation: CAA39235.1.
PIR	S19685.
3D structure databases
HSSP	HSSP built from PDB template 1DXL based on UniProtKB P31023.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 403.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. 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]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH3_PSEPU

Accession

Primary (citable) accession number: P31046

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 75 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)