[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Leaf; PubMed=1541297 [NCBI, ExPASy, EBI, Israel, Japan] Bourguignon J., Macherel D., Neuburger M., Douce R.; "Isolation, characterization, and sequence analysis of a cDNA clone encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria."; Eur. J. Biochem. 204:865-873(1992).
[2]	SEQUENCE REVISION TO 480. Bourguignon J.; Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Birte; TISSUE=Leaf; PubMed=1560008 [NCBI, ExPASy, EBI, Israel, Japan] Turner S.R., Ireland R., Rawsthorne S.; "Purification and primary amino acid sequence of the L subunit of glycine decarboxylase. Evidence for a single lipoamide dehydrogenase in plant mitochondria."; J. Biol. Chem. 267:7745-7750(1992).
[4]	SEQUENCE REVISION TO 499-501. Rawsthorne S.; Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[5]	PROTEIN SEQUENCE OF 32-61 AND 493-501, AND MASS SPECTROMETRY. PubMed=8546688 [NCBI, ExPASy, EBI, Israel, Japan] Bourguignon J., Merand V., Rawsthorne S., Forest E., Douce R.; "Glycine decarboxylase and pyruvate dehydrogenase complexes share the same dihydrolipoamide dehydrogenase in pea leaf mitochondria: evidence from mass spectrometry and primary-structure analysis."; Biochem. J. 313:229-234(1996).
[6]	X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 32-501 IN COMPLEX WITH FAD, SUBUNIT, AND DISULFIDE BOND. PubMed=10806386 [NCBI, ExPASy, EBI, Israel, Japan] Faure M., Bourguignon J., Neuburger M., MacHerel D., Sieker L., Ober R., Kahn R., Cohen-Addad C., Douce R.; "Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins."; Eur. J. Biochem. 267:2890-2898(2000).
[7]	ERRATUM. Faure M., Bourguignon J., Neuburger M., MacHerel D., Sieker L., Ober R., Kahn R., Cohen-Addad C., Douce R.; Eur. J. Biochem. 267:3914-3914(2000).

Comments

FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. The pyruvate dehydrogenase complex contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
CATALYTIC ACTIVITY: Protein N⁶-(dihydrolipoyl)lysine + NAD⁺ = protein N⁶-(lipoyl)lysine + NADH.
COFACTOR: Binds 1 FAD per subunit.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
MASS SPECTROMETRY: Mass=49753; Mass_error=5; Method=Electrospray; Range=32-501; Source=PubMed:8546688;.
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

X63464; CAA45066.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X62995; CAA44729.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S22384; S22384.

3D structure databases

PDB

1DXL; X-ray; 3.15 A; A/B/C/D=32-501.

[ExPASy / RCSB / EBI]

PDBsum

1DXL; -.

ModBase

P31023.

Protein-protein interaction databases

IntAct

P31023; -.

Ontologies

GO:0005960;	Cellular component: glycine cleavage complex (inferred from direct assay from UniProtKB).
GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
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: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

3D-structure; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Redox-active center; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 31`	`31`	`Mitochondrion.`
`CHAIN`	`32 501`	`470`	`Dihydrolipoyl dehydrogenase, mitochondrial.`	`PRO_0000030299`
`NP_BIND`	`67 76`	`10`	`FAD.`
`NP_BIND`	`178 180`	`3`	`FAD (By similarity).`
`NP_BIND`	`215 222`	`8`	`NAD (By similarity).`
`NP_BIND`	`354 357`	`4`	`FAD.`
`ACT_SITE`	`480 480`		`Proton acceptor (By similarity).`
`BINDING`	`85 85`		`FAD (By similarity).`
`BINDING`	`149 149`		`FAD; via amide nitrogen and carbonyl oxygen.`
`BINDING`	`238 238`		`NAD (By similarity).`
`BINDING`	`272 272`		`NAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`307 307`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`348 348`		`FAD.`
`DISULFID`	`76 81`		`Redox-active.`
`STRAND`	`40 43`	`4`
`HELIX`	`47 58`	`12`
`STRAND`	`63 67`	`5`
`STRAND`	`69 72`	`4`
`HELIX`	`76 79`	`4`
`HELIX`	`81 99`	`19`
`HELIX`	`102 104`	`3`
`STRAND`	`106 109`	`4`
`STRAND`	`111 113`	`3`
`HELIX`	`115 140`	`26`
`STRAND`	`143 147`	`5`
`STRAND`	`149 153`	`5`
`STRAND`	`156 159`	`4`
`STRAND`	`162 164`	`3`
`STRAND`	`167 170`	`4`
`STRAND`	`172 176`	`5`
`STRAND`	`180 182`	`3`
`STRAND`	`192 196`	`5`
`HELIX`	`198 201`	`4`
`STRAND`	`209 214`	`6`
`HELIX`	`218 230`	`13`
`STRAND`	`233 237`	`5`
`STRAND`	`239 244`	`6`
`HELIX`	`249 261`	`13`
`STRAND`	`269 276`	`8`
`STRAND`	`278 291`	`14`
`STRAND`	`295 303`	`9`
`STRAND`	`308 310`	`3`
`TURN`	`318 321`	`4`
`STRAND`	`326 328`	`3`
`STRAND`	`343 345`	`3`
`STRAND`	`350 352`	`3`
`HELIX`	`356 370`	`15`
`STRAND`	`384 386`	`3`
`STRAND`	`388 396`	`9`
`HELIX`	`399 404`	`6`
`STRAND`	`409 415`	`7`
`HELIX`	`416 418`	`3`
`HELIX`	`420 425`	`6`
`STRAND`	`431 437`	`7`
`TURN`	`438 440`	`3`
`STRAND`	`442 450`	`9`
`HELIX`	`453 465`	`13`
`HELIX`	`470 474`	`5`
`HELIX`	`485 495`	`11`

Sequence information

Length: 501 AA [This is the length of the unprocessed precursor]

Molecular weight: 53310 Da [This is the MW of the unprocessed precursor]

CRC64: 639D2D6368589FCE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAMANLARRK GYSLLSSETL RYSFSLRSRA FASGSDENDV VIIGGGPGGY VAAIKAAQLG 

        70         80         90        100        110        120 
FKTTCIEKRG ALGGTCLNVG CIPSKALLHS SHMYHEAKHS FANHGVKVSN VEIDLAAMMG 

       130        140        150        160        170        180 
QKDKAVSNLT RGIEGLFKKN KVTYVKGYGK FVSPSEISVD TIEGENTVVK GKHIIIATGS 

       190        200        210        220        230        240 
DVKSLPGVTI DEKKIVSSTG ALALSEIPKK LVVIGAGYIG LEMGSVWGRI GSEVTVVEFA 

       250        260        270        280        290        300 
SEIVPTMDAE IRKQFQRSLE KQGMKFKLKT KVVGVDTSGD GVKLTVEPSA GGEQTIIEAD 

       310        320        330        340        350        360 
VVLVSAGRTP FTSGLNLDKI GVETDKLGRI LVNERFSTNV SGVYAIGDVI PGPMLAHKAE 

       370        380        390        400        410        420 
EDGVACVEYL AGKVGHVDYD KVPGVVYTNP EVASVGKTEE QVKETGVEYR VGKFPFMANS 

       430        440        450        460        470        480 
RAKAIDNAEG LVKIIAEKET DKILGVHIMA PNAGELIHEA AIALQYDASS EDIARVCHAH 

       490        500 
PTMSEAIKEA AMATYDKPIH I

P31023 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