[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=G2; PubMed=3046941 [NCBI, ExPASy, EBI, Israel, Japan] Burns G., Brown T., Hatter K., Sokatch J.R.; "Comparison of the amino acid sequences of the transacylase components of branched chain oxoacid dehydrogenase of Pseudomonas putida, and the pyruvate and 2-oxoglutarate dehydrogenases of Escherichia coli."; Eur. J. Biochem. 176:165-169(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=G2; PubMed=2917566 [NCBI, ExPASy, EBI, Israel, Japan] Burns G., Brown T., Hatter K., Sokatch J.R.; "Sequence analysis of the lpdV gene for lipoamide dehydrogenase of branched-chain-oxoacid dehydrogenase of Pseudomonas putida."; Eur. J. Biochem. 179:61-69(1989).
[3]	X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH NAD AND FAD, SUBUNIT, AND DISULFIDE BOND. DOI=10.1002/prot.340130406; PubMed=1325638 [NCBI, ExPASy, EBI, Israel, Japan] Mattevi A., Obmolova G., Sokatsch J.R., Betzel C., Hol W.G.J.; "The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45-A resolution."; Proteins 13:336-351(1992).

Comments

FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
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

M57613; AAA65618.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S02139; DEPSLP.

3D structure databases

PDB

1LVL; X-ray; 2.45 A; A=2-459.

[ExPASy / RCSB / EBI]

PDBsum

1LVL; -.

ModBase

P09063.

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: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

P09063; -.

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

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 459`	`459`	`Dihydrolipoyl dehydrogenase.`	`PRO_0000068038`
`NP_BIND`	`36 44`	`9`	`FAD.`
`NP_BIND`	`179 183`	`5`	`NAD.`
`NP_BIND`	`264 267`	`4`	`NAD.`
`ACT_SITE`	`438 438`		`Proton acceptor (By similarity).`
`BINDING`	`53 53`		`FAD.`
`BINDING`	`119 119`		`FAD; via amide nitrogen and carbonyl oxygen.`
`BINDING`	`142 142`		`FAD; via carbonyl oxygen.`
`BINDING`	`182 182`		`FAD.`
`BINDING`	`202 202`		`NAD.`
`BINDING`	`236 236`		`NAD; via amide nitrogen.`
`BINDING`	`306 306`		`FAD; via amide nitrogen.`
`BINDING`	`312 312`		`NAD; via carbonyl oxygen.`
`BINDING`	`314 314`		`FAD; via amide nitrogen.`
`DISULFID`	`44 49`		`Redox-active.`
`STRAND`	`8 12`	`5`
`HELIX`	`16 28`	`13`
`STRAND`	`32 35`	`4`
`HELIX`	`42 47`	`6`
`HELIX`	`49 67`	`19`
`STRAND`	`76 83`	`8`
`HELIX`	`85 109`	`25`
`STRAND`	`113 115`	`3`
`STRAND`	`119 123`	`5`
`STRAND`	`126 129`	`4`
`STRAND`	`132 135`	`4`
`STRAND`	`137 141`	`5`
`STRAND`	`145 147`	`3`
`HELIX`	`162 165`	`4`
`STRAND`	`173 178`	`6`
`HELIX`	`182 194`	`13`
`STRAND`	`197 201`	`5`
`STRAND`	`203 208`	`6`
`HELIX`	`213 226`	`14`
`STRAND`	`229 231`	`3`
`STRAND`	`235 240`	`6`
`STRAND`	`243 247`	`5`
`STRAND`	`249 251`	`3`
`STRAND`	`261 263`	`3`
`STRAND`	`267 269`	`3`
`STRAND`	`272 275`	`4`
`HELIX`	`276 278`	`3`
`STRAND`	`301 303`	`3`
`HELIX`	`305 308`	`4`
`HELIX`	`314 328`	`15`
`STRAND`	`342 344`	`3`
`STRAND`	`346 354`	`9`
`HELIX`	`357 362`	`6`
`STRAND`	`367 373`	`7`
`HELIX`	`374 376`	`3`
`HELIX`	`378 382`	`5`
`STRAND`	`389 395`	`7`
`TURN`	`396 398`	`3`
`STRAND`	`400 408`	`9`
`HELIX`	`411 413`	`3`
`HELIX`	`414 424`	`11`
`HELIX`	`428 432`	`5`
`HELIX`	`443 452`	`10`

Sequence information

Length: 459 AA [This is the length of the unprocessed precursor]

Molecular weight: 48159 Da [This is the MW of the unprocessed precursor]

CRC64: 3D60A7DE167D0586 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQQTIQTTLL IIGGGPGGYV AAIRAGQLGI PTVLVEGQAL GGTCLNIGCI PSKALIHVAE 

        70         80         90        100        110        120 
QFHQASRFTE PSPLGISVAS PRLDIGQSVA WKDGIVDRLT TGVAALLKKH GVKVVHGWAK 

       130        140        150        160        170        180 
VLDGKQVEVD GQRIQCEHLL LATGSSSVEL PMLPLGGPVI SSTEALAPKA LPQHLVVVGG 

       190        200        210        220        230        240 
GYIGLELGIA YRKLGAQVSV VEARERILPT YDSELTAPVA ESLKKLGIAL HLGHSVEGYE 

       250        260        270        280        290        300 
NGCLLANDGK GGQLRLEADR VLVAVGRRPR TKGFNLECLD LKMNGAAIAI DERCQTSMHN 

       310        320        330        340        350        360 
VWAIGDVAGE PMLAHRAMAQ GEMVAEIIAG KARRFEPAAI AAVCFTDPEV VVVGKTPEQA 

       370        380        390        400        410        420 
SQQGLDCIVA QFPFAANGRA MSLESKSGFV RVVARRDNHL ILGWQAVGVA VSELSTAFAQ 

       430        440        450 
SLEMGACLED VAGTIHAHPT LGEAVQEAAL RALGHALHI

P09063 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