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Q01205 (ODO2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length454 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 Ref.2 Ref.3
Chain69 – 454386Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
PRO_0000020475

Regions

Domain72 – 14473Lipoyl-binding

Sites

Active site4251 Potential
Active site4291 Potential

Amino acid modifications

Modified residue1111N6-lipoyllysine Potential

Experimental info

Sequence conflict131S → M in BAA14397. Ref.2
Sequence conflict52 – 543NSS → TVA in BAA14397. Ref.2
Sequence conflict1641Y → H in BAA14397. Ref.2
Sequence conflict2811F → L in BAA14397. Ref.2
Sequence conflict4481R → A in BAA14397. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q01205 [UniParc].

Last modified April 12, 2005. Version 2.
Checksum: 2818F530F4B7C683

FASTA45448,925
        10         20         30         40         50         60 
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPDSRKMVI NNSSVFSVRF 

        70         80         90        100        110        120 
FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE DEVVCEIETD KTSVQVPSPA 

       130        140        150        160        170        180 
NGIIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAEAP ATAYKAAPEA PAAPPPPVAP 

       190        200        210        220        230        240 
VPTQMPPVPS PSQPPSSKPV SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK 

       250        260        270        280        290        300 
EAQNTCAMLT TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN 

       310        320        330        340        350        360 
AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE LGEKARKNEL 

       370        380        390        400        410        420 
AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHGI FDRPVAVGGK VEVRPMMYVA 

       430        440        450 
LTYDHRLIDG REAVTFLRKI KAAVEDPRVL LLDL

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[2]"Purification and molecular cloning of succinyltransferase of the rat alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif of the putative E3 and/or E1 binding site."
Nakano K., Matuda S., Yamanaka T., Tsubouchi H., Nakagawa S., Titani K., Ohta S., Miyata T.
J. Biol. Chem. 266:19013-19017(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-454, PROTEIN SEQUENCE OF 69-83.
Tissue: Heart.
[3]Lubec G., Chen W.-Q., Afjehi-Sadat L., Diao W.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 69-89; 135-145; 262-308 AND 314-326, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC083858 mRNA. Translation: AAH83858.1.
D90401 mRNA. Translation: BAA14397.1.
IPIIPI00551702.
PIRA41015.
RefSeqNP_001006982.2. NM_001006981.2.
UniGeneRn.99702.

3D structure databases

ProteinModelPortalQ01205.
SMRQ01205. Positions 221-454.
ModBaseSearch...

Protein-protein interaction databases

IntActQ01205. 1 interaction.

PTM databases

PhosphoSiteQ01205.

Proteomic databases

PaxDbQ01205.
PRIDEQ01205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID299201.
KEGGrno:299201.
UCSCRGD:1359615. rat.

Organism-specific databases

CTD1743.
RGD1359615. Dlst.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
HOVERGENHBG000268.
InParanoidQ01205.
KOK00658.
OrthoDBEOG4B2SZ1.

Enzyme and pathway databases

BRENDA2.3.1.61. 5301.
UniPathwayUPA00868; UER00840.

Gene expression databases

ArrayExpressQ01205.
GenevestigatorQ01205.
GermOnlineENSRNOG00000005061. Rattus norvegicus.

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

NextBio644993.

Entry information

Entry nameODO2_RAT
AccessionPrimary (citable) accession number: Q01205
Secondary accession number(s): Q5XI35
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 12, 2005
Last modified: April 3, 2013
This is version 119 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