[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3693355 [NCBI, ExPASy, EBI, Israel, Japan] Otulakowski G., Robinson B.H.; "Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases."; J. Biol. Chem. 262:17313-17318(1987).
[2]	PROTEIN SEQUENCE OF 36-89; 91-104; 317-331; 346-360; 388-417 AND 450-482. TISSUE=Heart; PubMed=6954534 [NCBI, ExPASy, EBI, Israel, Japan] Williams C.H. Jr., Arscott L.D., Schulz G.E.; "Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase."; Proc. Natl. Acad. Sci. U.S.A. 79:2199-2201(1982).

Comments

FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes.
CATALYTIC ACTIVITY: Protein N⁶-(dihydrolipoyl)lysine + NAD⁺ = protein N⁶-(lipoyl)lysine + NADH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds (By similarity). Homodimer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
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

J03489; AAA31069.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A28448; DEPGLP.

NP_999227.1; -.

3D structure databases

HSSP

P09624; 1JEH. [HSSP ENTRY / PDB]

SMR

P09623; 37-509.

ModBase

P09623.

Ontologies

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: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.

Genome annotation databases

GeneID

397129; -.

KEGG

ssc:397129; -.

Phylogenomic databases

HOVERGEN

P09623; -.

Other

ProtoNet

P09623.

UniRef

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

Keywords

Acetylation; 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 35`	`35`	`Mitochondrion.`
`CHAIN`	`36 509`	`474`	`Dihydrolipoyl dehydrogenase, mitochondrial.`	`PRO_0000030298`
`NP_BIND`	`71 80`	`10`	`FAD (By similarity).`
`NP_BIND`	`183 185`	`3`	`FAD (By similarity).`
`NP_BIND`	`220 227`	`8`	`NAD (By similarity).`
`NP_BIND`	`361 364`	`4`	`FAD (By similarity).`
`ACT_SITE`	`487 487`		`Proton acceptor (By similarity).`
`BINDING`	`89 89`		`FAD (By similarity).`
`BINDING`	`154 154`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`243 243`		`NAD (By similarity).`
`BINDING`	`278 278`		`NAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`314 314`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`355 355`		`FAD (By similarity).`
`MOD_RES`	`127 127`		`N6-acetyllysine (By similarity).`
`DISULFID`	`80 85`		`Redox-active (By similarity).`
`CONFLICT`	`95 97`		`SHY -> GHA (in Ref. 2; AA sequence).`
`CONFLICT`	`346 346`		`K -> R (in Ref. 2; AA sequence).`
`CONFLICT`	`351 351`		`Y -> A (in Ref. 2; AA sequence).`

Sequence information

Length: 509 AA [This is the length of the unprocessed precursor]

Molecular weight: 54185 Da [This is the MW of the unprocessed precursor]

CRC64: 38A0469FED071300 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQSWSRVYCT LAKRGHFNRI AHGLQGVSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA 

        70         80         90        100        110        120 
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL 

       130        140        150        160        170        180 
EKMMEQKSNA VKALTGGIAH LFKQNKVVRV NGYGKITGKN QVTATKADGS TEVINTKNIL 

       190        200        210        220        230        240 
IATGSEVTPF PGITIDEDTV VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT 

       250        260        270        280        290        300 
AVELLGHVGG IGIDMEVSKN FQRILQKQGF KFKLNTKVIG ATKKSDGNID VSIEAASGGK 

       310        320        330        340        350        360 
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP 

       370        380        390        400        410        420 
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK 

       430        440        450        460        470        480 
FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHIIGPGA GEMINEAALA LEYGASCEDI 

       490        500 
ARVCHAHPTL SEAFREANLA ASFGKAINF

P09623 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