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P83708 (ODO2_DELAC) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

EC=2.3.1.61
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name=OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene names
Name:sucB
OrganismDelftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans)
Taxonomic identifier80866 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeDelftia

Protein attributes

Sequence length12 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. UniProtKB P52993

Catalytic activity

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity. UniProtKB P52993

Induction

By 2,4-dichlorophenol. Ref.1

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›12›12Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162254

Regions

Domain1 – ›12›12Lipoyl-binding

Experimental info

Non-terminal residue121

Sequences

Sequence LengthMass (Da)Tools
P83708 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: D0593347F272C322

FASTA121,319
        10 
AIVEVKVPXL XE 

« Hide

References

[1]"Regulation of catabolic enzymes during long-term exposure of Delftia acidovorans MC1 to chlorophenoxy herbicides."
Benndorf D., Davidson I., Babel W.
Microbiology 150:1005-1014(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, INDUCTION BY 2,4-DICHLOROPHENOL.
Strain: MC1.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00868; UER00840.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameODO2_DELAC
AccessionPrimary (citable) accession number: P83708
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 15, 2003
Last modified: March 19, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways