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

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 N⁶-(dihydrolipoyl)lysine + NAD⁺ = protein N⁶-(lipoyl)lysine + NADH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X55704; CAA39235.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S19685; S19685.

3D structure databases

HSSP

P31023; 1DXL. [HSSP ENTRY / PDB]

ModBase

P31046.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004148;	Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR006258; Lipoamide_DHase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

PANTHER

PTHR22912:SF20; Lipoamide_DH; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01350; lipoamide_DH; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 466`	`466`	`Dihydrolipoyl dehydrogenase 3.`	`PRO_0000068040`
`NP_BIND`	`33 42`	`10`	`FAD (By similarity).`
`NP_BIND`	`181 185`	`5`	`NAD (By similarity).`
`NP_BIND`	`271 274`	`4`	`NAD (By similarity).`
`ACT_SITE`	`445 445`		`Proton acceptor (By similarity).`
`BINDING`	`51 51`		`FAD (By similarity).`
`BINDING`	`115 115`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`204 204`		`NAD (By similarity).`
`BINDING`	`238 238`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`313 313`		`FAD (By similarity).`
`BINDING`	`321 321`		`FAD; via amide nitrogen (By similarity).`
`DISULFID`	`42 47`		`Redox-active (By similarity).`

Sequence information

Length: 466 AA [This is the length of the unprocessed precursor]

Molecular weight: 49257 Da [This is the MW of the unprocessed precursor]

CRC64: E805AC5E879881F3 [This is a checksum on the sequence]

        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

P31046 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools