[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. DOI=10.1104/pp.127.2.615; PubMed=11598235 [NCBI, ExPASy, EBI, Israel, Japan] Lutziger I., Oliver D.J.; "Characterization of two cDNAs encoding mitochondrial lipoamide dehydrogenase from Arabidopsis."; Plant Physiol. 127:615-623(2001).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/7.2.131; PubMed=10819329 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."; DNA Res. 7:131-135(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). STRAIN=cv. Columbia; Shinn P., Chen H., Kim C.J., Ecker J.R.; "Arabidopsis ORF clones."; Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.; "Full-length cDNA from Arabidopsis thaliana."; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 36-507 (ISOFORM 1). STRAIN=cv. Columbia; Machuy N., Klein M., Mueller-Roeber B.; "Cloning and characterization of 2-oxoglutarate dehydrogenase from Arabidopsis thaliana."; Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[6]	IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan] Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.; "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."; Plant Cell 16:241-256(2004).
[7]	FUNCTION. DOI=10.1104/pp.103.035675; PubMed=14764908 [NCBI, ExPASy, EBI, Israel, Japan] Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.; "Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis."; Plant Physiol. 134:838-848(2004).

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 (By similarity).
SUBUNIT: Homodimer (By similarity).
INTERACTION:
O23320:CML8; NbExp=1; IntAct=EBI-1237919, EBI-1237764;
SUBCELLULAR LOCATION: Mitochondrion matrix.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q9M5K2-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q9M5K2-2
Note: May be due to an intron retention. No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_021588, VSP_021589.

TISSUE SPECIFICITY: Preferentially expressed in roots, flowers and siliques and at a lower level in stems and leaves.
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

AF228640; AAF34796.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB022216; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BT024578; ABD38917.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087203; AAM64759.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ223804; CAA11554.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_566570.3; -.
NP_851005.1; -.

UniGene

At.20793

3D structure databases

HSSP

P31023; 1DXL. [HSSP ENTRY / PDB]

SMR

Q9M5K2; 41-507.

ModBase

Q9M5K2.

Protein-protein interaction databases

IntAct

Q9M5K2; -.

Organism-specific databases

GeneFarm

4375; 442.

TAIR

At3g17240; -.

Gene expression databases

GermOnline

AT3G17240; Arabidopsis thaliana.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from direct assay from TAIR).
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:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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).
GO:0046686;	Biological process: response to cadmium ion (inferred from direct assay from TAIR).
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.

ProtoNet

Q9M5K2.

Genome annotation databases

GeneID

820984; -.

GenomeReviews

BA000014_GR; AT3G17240.

KEGG

ath:AT3G17240; -.

NMPDR

fig|3702.1.peg.13912; -.

Other

UniRef

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

Keywords

Alternative splicing; Complete proteome; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Redox-active center; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 36`	`36`	`Mitochondrion (Potential).`
`CHAIN`	`37 507`	`471`	`Dihydrolipoyl dehydrogenase 2, mitochondrial.`	`PRO_0000260230`
`NP_BIND`	`73 82`	`10`	`FAD (By similarity).`
`NP_BIND`	`184 186`	`3`	`FAD (By similarity).`
`NP_BIND`	`221 228`	`8`	`NAD (By similarity).`
`NP_BIND`	`360 363`	`4`	`FAD (By similarity).`
`ACT_SITE`	`486 486`		`Proton acceptor (By similarity).`
`BINDING`	`91 91`		`FAD (By similarity).`
`BINDING`	`155 155`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`244 244`		`NAD (By similarity).`
`BINDING`	`278 278`		`NAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`313 313`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`354 354`		`FAD (By similarity).`
`DISULFID`	`82 87`		`Redox-active (By similarity).`
`VAR_SEQ`	`92 127`		`ALLHSSHMYHEAKHVFANHGVKVSSVEVDLPAMLAQ -> VILETPFPITLIRRKFSPIFIRLLWNLLVDHHLDSI (in isoform 2).`	`VSP_021588`
`VAR_SEQ`	`128 507`		`Missing (in isoform 2).`	`VSP_021589`

Sequence information

Length: 507 AA [This is the length of the unprocessed precursor]

Molecular weight: 53986 Da [This is the MW of the unprocessed precursor]

CRC64: C5CA38074A8103D7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAMASLARRK AYFLTRNISN SPTDAFRFSF SLTRGFASSG SDDNDVVIIG GGPGGYVAAI 

        70         80         90        100        110        120 
KAAQLGLKTT CIEKRGALGG TCLNVGCIPS KALLHSSHMY HEAKHVFANH GVKVSSVEVD 

       130        140        150        160        170        180 
LPAMLAQKDT AVKNLTRGVE GLFKKNKVNY VKGYGKFLSP SEVSVDTIDG ENVVVKGKHI 

       190        200        210        220        230        240 
IVATGSDVKS LPGITIDEKK IVSSTGALSL TEIPKKLIVI GAGYIGLEMG SVWGRLGSEV 

       250        260        270        280        290        300 
TVVEFAADIV PAMDGEIRKQ FQRSLEKQKM KFMLKTKVVG VDSSGDGVKL IVEPAEGGEQ 

       310        320        330        340        350        360 
TTLEADVVLV SAGRTPFTSG LDLEKIGVET DKGGRILVNE RFSTNVSGVY AIGDVIPGPM 

       370        380        390        400        410        420 
LAHKAEEDGV ACVEFIAGKH GHVDYDKVPG VVYTYPEVAS VGKTEEQLKK EGVSYNVGKF 

       430        440        450        460        470        480 
PFMANSRAKA IDTAEGMVKI LADKETDKIL GVHIMSPNAG ELIHEAVLAI NYDASSEDIA 

       490        500 
RVCHAHPTMS EAIKEAAMAT YDKPIHM

Q9M5K2 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