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Q9N0F1 (ODO2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. 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
E2o
Short name=PE2o
Gene names
Name:DLST
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

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). Ref.1

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.

Subcellular location

Mitochondrion Ref.1.

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
Chain69 – 455387Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
PRO_0000020474

Regions

Domain72 – 14473Lipoyl-binding
Region221 – 453233Catalytic
Compositional bias151 – 21565Pro-rich

Sites

Active site4261 Potential
Active site4301 Potential

Amino acid modifications

Modified residue1111N6-lipoyllysine Potential
Modified residue1551N6-acetyllysine By similarity
Modified residue2691N6-acetyllysine By similarity
Modified residue2741N6-acetyllysine By similarity
Modified residue2751N6-acetyllysine By similarity
Modified residue2791N6-acetyllysine By similarity
Modified residue3091N6-acetyllysine By similarity

Experimental info

Mutagenesis3741S → A: Loss of activity.
Mutagenesis4261H → C: 16% of activity.
Mutagenesis4301D → A, E or N: Loss of activity.
Mutagenesis451 – 4533LLL → AAA or DDD: Loss of activity.

Sequences

Sequence LengthMass (Da)Tools
Q9N0F1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 563B5E7455C842FA

FASTA45548,977
        10         20         30         40         50         60 
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGISLCQGP GYPDSRKIVI SNSSVLNVRF 

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

       130        140        150        160        170        180 
NGVIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAEAP AAAAPKAEPA VSAVPPPPAA 

       190        200        210        220        230        240 
SIPTQMPPVP SPPQPLTSKP VSAVKPTAAP PVAEPGAVKG LRAEHREKMN RMRQRIAQRL 

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

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

       370        380        390        400        410        420 
LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA IVDRPVAVGG KVEIRPMMYV 

       430        440        450 
ALTYDHRLID GREAVTFLRK IKAAVEDPRV LLLDL 

« Hide

References

[1]"Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex."
Koike K., Suematsu T., Ehara M.
Eur. J. Biochem. 267:3005-3016(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS.
Tissue: Brain cortex and Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB035206 mRNA. Translation: BAA95700.1.
RefSeqNP_999562.1. NM_214397.1.
UniGeneSsc.2730.

3D structure databases

ProteinModelPortalQ9N0F1.
SMRQ9N0F1. Positions 222-455.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9N0F1.
PRIDEQ9N0F1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000002639; ENSSSCP00000002572; ENSSSCG00000002374.
GeneID397690.
KEGGssc:397690.

Organism-specific databases

CTD1743.

Phylogenomic databases

eggNOGCOG0508.
GeneTreeENSGT00740000115255.
HOGENOMHOG000281563.
HOVERGENHBG000268.
KOK00658.
OMAAEDEVIC.
OrthoDBEOG78PV93.
TreeFamTF314164.

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...

Entry information

Entry nameODO2_PIG
AccessionPrimary (citable) accession number: Q9N0F1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 93 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