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Reviewed, UniProtKB/Swiss-Prot P31023 (DLDH_PEA)

Last modified February 9, 2010. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dihydrolipoyl dehydrogenase, mitochondrial
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    Pyruvate dehydrogenase complex E3 subunit
      Short name=PDC-E3
      Short name=E3
    Glycine cleavage system L protein
Gene names
Name: LPD
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

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Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (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 N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homodimer. Ref.6

Subcellular location

Mitochondrion matrix.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Mass spectrometry

Molecular mass is 49753±5 Da from positions 32 - 501. Determined by ESI. Ref.5

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3131Mitochondrion Ref.5
Chain32 – 501470Dihydrolipoyl dehydrogenase, mitochondrial
PRO_0000030299

Regions

Nucleotide binding67 – 7610FAD
Nucleotide binding178 – 1803FAD By similarity
Nucleotide binding215 – 2228NAD By similarity
Nucleotide binding354 – 3574FAD

Sites

Active site4801Proton acceptor By similarity
Binding site851FAD By similarity
Binding site1491FAD; via amide nitrogen and carbonyl oxygen
Binding site2381NAD By similarity
Binding site2721NAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3071NAD; via amide nitrogen By similarity
Binding site3481FAD

Amino acid modifications

Disulfide bond76 ↔ 81Redox-active Ref.6

Secondary structure

1 ......................................................................................... 501
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P31023-1 [UniParc].

Last modified July 11, 2001. Version 2.
Checksum: 639D2D6368589FCE

FASTA50153,310
        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

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References

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

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X63464 mRNA. Translation: CAA45066.2.
X62995 mRNA. Translation: CAA44729.1.
PIRS22384.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXLX-ray3.15A/B/C/D32-501[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP31023. 1 interaction.

Enzyme and pathway databases

BRENDA1.8.1.4. 287.

Family and domain databases

InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF20. Lipoamide_DH. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDLDH_PEA
AccessionPrimary (citable) accession number: P31023
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 11, 2001
Last modified: February 9, 2010
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents