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Reviewed, UniProtKB/Swiss-Prot P84545 (DLDH_POPEU)

Last modified January 20, 2009. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
OrganismPopulus euphratica (Euphrates poplar)
Taxonomic identifier75702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IMalpighialesSalicaceaeSaliceaePopulus

Protein attributes

Sequence length11 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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) By similarity. UniProtKB P09622

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. UniProtKB P09622

Cofactor

Binds 1 FAD per subunit By similarity. UniProtKB P14218

Subunit structure

Homodimer By similarity. UniProtKB P09622

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

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

Ontologies

Keywords
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiondihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›11›11Dihydrolipoyl dehydrogenase
PRO_0000068011

Experimental info

Non-terminal residue11
Non-terminal residue111

Sequences

Sequence LengthMass (Da)Tools
P84545-1 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: C2E56DC3D7273769

FASTA111,201
        10 
VGKFPLLANS R 

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References

[1]"Proteome profiling of Populus euphratica Oliv. upon heat stress."
Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S., Roepstorff P., Pais M.S.
Ann. Bot. 98:361-377(2006) [PubMed: 16740589] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Leaf.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.8.1.4. 293088.

Family and domain databases

InterProIPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PROSITEPS00076. PYRIDINE_REDOX_1. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH_POPEU
AccessionPrimary (citable) accession number: P84545
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: January 20, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

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