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Protein

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

Gene

Dlst

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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.

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.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Alpha-aminoadipic semialdehyde synthase, mitochondrial (Aass)
  2. Alpha-aminoadipic semialdehyde synthase, mitochondrial (Aass)
  3. no protein annotated in this organism
  4. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Aadat)
  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 sitei425Sequence analysis1
Active sitei429Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-71064. Lysine catabolism.
R-MMU-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Dlst
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1926170. Dlst.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleus Source: MGI
  • oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176822.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 68MitochondrionBy similarityAdd BLAST68
ChainiPRO_000002047369 – 454Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST386

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei82PhosphoserineCombined sources1
Modified residuei111N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei155N6-acetyllysineCombined sources1
Modified residuei268N6-acetyllysineCombined sources1
Modified residuei273N6-acetyllysineCombined sources1
Modified residuei274N6-acetyllysineCombined sources1
Modified residuei278N6-acetyllysineCombined sources1
Modified residuei308N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9D2G2.
PaxDbiQ9D2G2.
PeptideAtlasiQ9D2G2.
PRIDEiQ9D2G2.
TopDownProteomicsiQ9D2G2-1. [Q9D2G2-1]
Q9D2G2-2. [Q9D2G2-2]

2D gel databases

REPRODUCTION-2DPAGEQ9D2G2.
UCD-2DPAGEQ9D2G2.

PTM databases

iPTMnetiQ9D2G2.
PhosphoSitePlusiQ9D2G2.
SwissPalmiQ9D2G2.

Expressioni

Gene expression databases

BgeeiENSMUSG00000004789.
GenevisibleiQ9D2G2. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi219707. 2 interactors.
IntActiQ9D2G2. 5 interactors.
MINTiMINT-1860129.
STRINGi10090.ENSMUSP00000060346.

Structurei

3D structure databases

ProteinModelPortaliQ9D2G2.
SMRiQ9D2G2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini71 – 145Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST75

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0559. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133844.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiQ9D2G2.
KOiK00658.
OMAiAKPAMHT.
OrthoDBiEOG091G08FX.
PhylomeDBiQ9D2G2.
TreeFamiTF314164.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9D2G2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCRGP GYPDNRKMVI
60 70 80 90 100
NSGSVFRVRF FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE
110 120 130 140 150
DEVVCEIETD KTSVQVPSPA NGIIEALLVP DGGKVEGGTP LFTLRKTGAA
160 170 180 190 200
PAKAKPAETP APAHKAEPAA PAAPPPPAAP VLTQMPPVPS PSQPPSSKPV
210 220 230 240 250
SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK EAQNTCAMLT
260 270 280 290 300
TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN
310 320 330 340 350
AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE
360 370 380 390 400
LGEKARKNEL AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHAI
410 420 430 440 450
FDRPVAVGGK VEVRPMMYVA LTYDHRLIDG REAVTFLRKI KAAVEDPRVL

LLDL
Length:454
Mass (Da):48,995
Last modified:June 1, 2001 - v1
Checksum:i9CB31698D185442A
GO
Isoform 2 (identifier: Q9D2G2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-253: Missing.
     254-257: EVDM → MTSL

Note: No experimental confirmation available.
Show »
Length:201
Mass (Da):22,230
Checksum:iD999AAE99C49D3D8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti276N → S in BAE29011 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0250151 – 253Missing in isoform 2. 1 PublicationAdd BLAST253
Alternative sequenceiVSP_025016254 – 257EVDM → MTSL in isoform 2. 1 Publication4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019713 mRNA. Translation: BAB31840.1.
AK054053 mRNA. Translation: BAC35637.1.
AK149664 mRNA. Translation: BAE29011.1.
AK158877 mRNA. Translation: BAE34709.1.
AK168570 mRNA. Translation: BAE40440.1.
AK169943 mRNA. Translation: BAE41472.1.
CT010197 mRNA. Translation: CAJ18405.1.
BC006702 mRNA. Translation: AAH06702.1.
BC024066 mRNA. Translation: AAH24066.1.
CCDSiCCDS26052.1. [Q9D2G2-1]
RefSeqiNP_084501.1. NM_030225.4. [Q9D2G2-1]
UniGeneiMm.296221.

Genome annotation databases

EnsembliENSMUST00000053811; ENSMUSP00000060346; ENSMUSG00000004789. [Q9D2G2-1]
GeneIDi78920.
KEGGimmu:78920.
UCSCiuc007ogj.2. mouse. [Q9D2G2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019713 mRNA. Translation: BAB31840.1.
AK054053 mRNA. Translation: BAC35637.1.
AK149664 mRNA. Translation: BAE29011.1.
AK158877 mRNA. Translation: BAE34709.1.
AK168570 mRNA. Translation: BAE40440.1.
AK169943 mRNA. Translation: BAE41472.1.
CT010197 mRNA. Translation: CAJ18405.1.
BC006702 mRNA. Translation: AAH06702.1.
BC024066 mRNA. Translation: AAH24066.1.
CCDSiCCDS26052.1. [Q9D2G2-1]
RefSeqiNP_084501.1. NM_030225.4. [Q9D2G2-1]
UniGeneiMm.296221.

3D structure databases

ProteinModelPortaliQ9D2G2.
SMRiQ9D2G2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219707. 2 interactors.
IntActiQ9D2G2. 5 interactors.
MINTiMINT-1860129.
STRINGi10090.ENSMUSP00000060346.

Chemistry databases

ChEMBLiCHEMBL2176822.

PTM databases

iPTMnetiQ9D2G2.
PhosphoSitePlusiQ9D2G2.
SwissPalmiQ9D2G2.

2D gel databases

REPRODUCTION-2DPAGEQ9D2G2.
UCD-2DPAGEQ9D2G2.

Proteomic databases

EPDiQ9D2G2.
PaxDbiQ9D2G2.
PeptideAtlasiQ9D2G2.
PRIDEiQ9D2G2.
TopDownProteomicsiQ9D2G2-1. [Q9D2G2-1]
Q9D2G2-2. [Q9D2G2-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053811; ENSMUSP00000060346; ENSMUSG00000004789. [Q9D2G2-1]
GeneIDi78920.
KEGGimmu:78920.
UCSCiuc007ogj.2. mouse. [Q9D2G2-1]

Organism-specific databases

CTDi1743.
MGIiMGI:1926170. Dlst.

Phylogenomic databases

eggNOGiKOG0559. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133844.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiQ9D2G2.
KOiK00658.
OMAiAKPAMHT.
OrthoDBiEOG091G08FX.
PhylomeDBiQ9D2G2.
TreeFamiTF314164.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-71064. Lysine catabolism.
R-MMU-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiDlst. mouse.
PROiQ9D2G2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004789.
GenevisibleiQ9D2G2. MM.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODO2_MOUSE
AccessioniPrimary (citable) accession number: Q9D2G2
Secondary accession number(s): Q3UEA0, Q4FK55, Q8CIE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.