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P86219 (ODO2_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 15. 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, mitochondrial

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
E2K
Gene names
Name:DLST
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length145 AA.
Sequence statusFragments.
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 Q01205

Catalytic activity

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine. UniProtKB Q01205

Cofactor

Binds 1 lipoyl cofactor covalently By similarity. UniProtKB Q01205

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6. UniProtKB Q01205

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity. UniProtKB Q01205

Subcellular location

Mitochondrion By similarity UniProtKB Q01205.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Gene Ontology (GO)
   Biological_processL-lysine catabolic process to acetyl-CoA via saccharopine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydrolipoyllysine-residue succinyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 145›145Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
PRO_0000394748

Regions

Domain4 – 3128Lipoyl-binding

Sites

Active site1191 Potential UniProtKB Q01205
Active site1231 Potential UniProtKB Q01205

Amino acid modifications

Modified residue361N6-acetyllysine By similarity
Modified residue661N6-acetyllysine By similarity

Experimental info

Non-adjacent residues21 – 222
Non-adjacent residues32 – 332
Non-adjacent residues104 – 1052
Non-adjacent residues132 – 1332
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P86219 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 32D674B5DD798BBD

FASTA14516,122
        10         20         30         40         50         60 
NDVITVQTPA FAESVTEGDV RVEGGTPLFT LRHNLKLGFM SAFVKASAFA LQEQPVVNAV 

        70         80         90        100        110        120 
IDDATKEVVY RDYIDISVAV ATPRGLVVPV IRNVETMNYA DIERVEVRPM MYVALTYDHR 

       130        140 
LIDGREAVTF LRAAVEDPRV LLLDL 

« Hide

References

[1]"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP86219.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00868; UER00840.

Family and domain databases

Gene3D3.30.559.10. 2 hits.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR023213. CAT-like_dom.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODO2_MESAU
AccessionPrimary (citable) accession number: P86219
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: February 19, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways