Skip Header

Contribute Send feedback
Read comments (?) or add your own

P11179 (ODO2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. 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
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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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).

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently.

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.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6868Mitochondrion By similarity
Chain69 – 455387Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
PRO_0000162252

Regions

Domain72 – 14473Lipoyl-binding

Sites

Active site4261 Potential
Active site4301 Potential

Amino acid modifications

Modified residue1111N6-lipoyllysine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11179 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: DB2124A4D06C389B

FASTA45548,973
        10         20         30         40         50         60 
MLSRSRCASR AFSRSLSAFQ KGNCPLVRRS LPGISLCQGP GYPDSRKTVI NSSNIFSVRF 

        70         80         90        100        110        120 
FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE DEVVCEIETD KTSVQVPSPA 

       130        140        150        160        170        180 
NGVIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAAAP AAAAPKAEPT VSAVPPPPAA 

       190        200        210        220        230        240 
PIPTQMPPVP SPSQPLTSKP VSAVKPTAAP PRAEAGAGVG LRSEHREKMN RMRQRIAQRL 

       250        260        270        280        290        300 
KEAQNTCAML TTFNEIDMSN IQEMRARHKD AFLKKHNLKL GFMSAFVKAS AFALQEQPVV 

       310        320        330        340        350        360 
NAVIDDATKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS ELGEKARKNE 

       370        380        390        400        410        420 
LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA IVDRPVVIGG KVEVRPMMYV 

       430        440        450 
ALTYDHRLID GREAVTFLRK IKAAVEDPRV LLLDL

« Hide

References

« Hide 'large scale' references
[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"Amino acid sequence surrounding the lipoic acid cofactor of bovine kidney 2-oxoglutarate dehydrogenase complex."
Bradford A.P., Aitken A., Beg F., Cook K.G., Yeaman S.J.
FEBS Lett. 222:211-214(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 107-122.
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BT026207 mRNA. Translation: ABG67046.1.
IPIIPI00692907.
PIRS00123.
RefSeqNP_001068750.1. NM_001075282.1.
UniGeneBt.41191.

3D structure databases

ProteinModelPortalP11179.
SMRP11179. Positions 226-452.
ModBaseSearch...

Protein-protein interaction databases

IntActP11179. 1 interaction.
STRING9913.ENSBTAP00000052502.

Proteomic databases

PaxDbP11179.
PRIDEP11179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID506888.
KEGGbta:506888.

Organism-specific databases

CTD1743.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
HOVERGENHBG000268.
KOK00658.

Enzyme and pathway databases

UniPathwayUPA00868; UER00840.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMSSF51230. Hybrid_motif. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20867785.

Entry information

Entry nameODO2_BOVIN
AccessionPrimary (citable) accession number: P11179
Secondary accession number(s): Q0V8L1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 17, 2006
Last modified: April 3, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents