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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

DLST

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi: L-lysine degradation via saccharopine pathway

This protein is involved in step 6 of the subpathway that synthesizes glutaryl-CoA from L-lysine.By similarity
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (DLST)
This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei119Sequence analysisBy similarity1
Active sitei123Sequence analysisBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialBy similarity (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2By similarity
Short name:
OGDC-E2By similarity
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complexBy similarity
E2KBy similarity
Gene namesi
Name:DLSTBy similarity
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

  • Mitochondrion By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000394748‹1 – 145Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST›145

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineBy similarity1
Modified residuei36N6-acetyllysineBy similarity1
Modified residuei66N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP86219.

Interactioni

Subunit structurei

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 31Lipoyl-bindingSequence analysisAdd BLAST28

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Sequence analysis
Contains 1 lipoyl-binding domain.Sequence analysis

Keywords - Domaini

Lipoyl

Family and domain databases

Gene3Di3.30.559.10. 2 hits.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR023213. CAT-like_dom.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragments.

P86219-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NDVITVQTPA FAESVTEGDV RVEGGTPLFT LRHNLKLGFM SAFVKASAFA
60 70 80 90 100
LQEQPVVNAV IDDATKEVVY RDYIDISVAV ATPRGLVVPV IRNVETMNYA
110 120 130 140
DIERVEVRPM MYVALTYDHR LIDGREAVTF LRAAVEDPRV LLLDL
Length:145
Mass (Da):16,122
Last modified:June 15, 2010 - v1
Checksum:i32D674B5DD798BBD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-adjacent residuesi21 – 22Curated2
Non-adjacent residuesi32 – 33Curated2
Non-adjacent residuesi104 – 105Curated2
Non-adjacent residuesi132 – 133Curated2

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP86219.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.

Family and domain databases

Gene3Di3.30.559.10. 2 hits.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR023213. CAT-like_dom.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODO2_MESAU
AccessioniPrimary (citable) accession number: P86219
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: October 14, 2015
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.