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Q869Y7 (ODO2_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:odhB
Synonyms:dlst
ORF Names:DDB_G0275029
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length439 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 three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

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.

Subcellular location

Mitochondrion By similarity.

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 – 4747Mitochondrion Potential
Chain48 – 439392Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
PRO_0000327966

Regions

Domain74 – 14774Lipoyl-binding
Compositional bias53 – 619Poly-Asn

Sites

Active site4101 By similarity
Active site4141 By similarity

Amino acid modifications

Modified residue1141N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q869Y7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 214DE063A7139A79

FASTA43947,633
        10         20         30         40         50         60 
MRSATKLIKN VNINRCVQSN VVRSTSRLIN NNSINTVRQF TSSSSSSFTS LFNNNNVNNT 

        70         80         90        100        110        120 
NIKYQRFYSS ANDVVIKVPS MGDSISEGTI VAWTKNVGDS VRVDEVVCSI ETDKVTIDIN 

       130        140        150        160        170        180 
APVSGTIVEL FAKEGENVTV GNDLYKIAKG EVAAAPKVEA PKAAEAPKAA APTPAPKAAE 

       190        200        210        220        230        240 
TPKAAPAPKS EAPTPAPKST TTTTSTGPSE TRVKMTRIRQ RTAQRLKDSQ NTAAMLTTFN 

       250        260        270        280        290        300 
ELDMSALMNM RKTYKDEFEK KHGVKFGFMS AFVKASTIAL KEQPIVNASV EENDIVYHNN 

       310        320        330        340        350        360 
VNINVAVSAP RGLVVPVIRN CENLSFADIE KEIGRLSGLA RNDALAIEDS IGGTFTISNG 

       370        380        390        400        410        420 
GVFGSMFGTP IINPPQSAIL GMHAIKDRPY VVNGQVVVRP IMYLALTYDH RIIDGREAVT 

       430 
FLKKIKDVLE NPERILLEL 

« Hide

References

[1]"Sequence and analysis of chromosome 2 of Dictyostelium discoideum."
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A.
Nature 418:79-85(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[3]"Identification of novel centrosomal proteins in Dictyostelium discoideum by comparative proteomic approaches."
Reinders Y., Schulz I., Graef R., Sickmann A.
J. Proteome Res. 5:589-598(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000013 Genomic DNA. Translation: EAL69795.1.

3D structure databases

ProteinModelPortalQ869Y7.
SMRQ869Y7. Positions 212-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ869Y7. 1 interaction.
STRING44689.DDB_0230198.

Proteomic databases

PRIDEQ869Y7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0230198; DDB0230198; DDB_G0275029.
KEGGddi:DDB_G0275029.

Organism-specific databases

dictyBaseDDB_G0275029. odhB.

Phylogenomic databases

eggNOGCOG0508.
KOK00658.
OMATSAQHAS.
PhylomeDBQ869Y7.
ProtClustDBPTZ00144.

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. SSF51230. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ869Y7.

Entry information

Entry nameODO2_DICDI
AccessionPrimary (citable) accession number: Q869Y7
Secondary accession number(s): Q553V8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase