UniProtKB - Q9D2G2 (ODO2_MOUSE)
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Dlst
Functioni
Catalytic activityi
- (R)-N6-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N6-(S8-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoABy similarityEC:2.3.1.61By similarityThis reaction proceeds in the backwardBy similarity direction.
Cofactori
: L-lysine degradation via saccharopine pathway Pathwayi
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:
- Lysine ketoglutarate reductase (Aass), Alpha-aminoadipic semialdehyde synthase, mitochondrial (Aass), Lysine ketoglutarate reductase (Aass)
- Lysine ketoglutarate reductase (Aass), Alpha-aminoadipic semialdehyde synthase, mitochondrial (Aass), Lysine ketoglutarate reductase (Aass)
- no protein annotated in this organism
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Aadat)
- no protein annotated in this organism
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (Dlst)
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.
Pathwayi: tricarboxylic acid cycle
This protein is involved in the pathway tricarboxylic acid cycle, which is part of Carbohydrate metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 425 | By similarity | 1 | |
Active sitei | 429 | By similarity | 1 |
GO - Molecular functioni
- chaperone binding Source: MGI
- dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB
- heat shock protein binding Source: MGI
- transferase activity, transferring acyl groups Source: UniProtKB
GO - Biological processi
- 2-oxoglutarate metabolic process Source: UniProtKB
- histone succinylation Source: UniProtKB
- L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
- NADH metabolic process Source: MGI
- succinyl-CoA metabolic process Source: UniProtKB
- tricarboxylic acid cycle Source: UniProtKB
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Tricarboxylic acid cycle |
Enzyme and pathway databases
Reactomei | R-MMU-389661, Glyoxylate metabolism and glycine degradation R-MMU-71064, Lysine catabolism R-MMU-71403, Citric acid cycle (TCA cycle) |
UniPathwayi | UPA00223 UPA00868;UER00840 |
Names & Taxonomyi
Protein namesi | Recommended name: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.61By similarity)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 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1926170, Dlst |
Subcellular locationi
Nucleus
- Nucleus By similarity
Mitochondrion
- Mitochondrion matrix By similarity
Note: Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation.By similarity
Mitochondrion
- mitochondrial matrix Source: UniProtKB-SubCell
- mitochondrion Source: MGI
Nucleus
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: MGI
Other locations
- intracellular membrane-bounded organelle Source: MGI
- myelin sheath Source: UniProtKB
- oxoglutarate dehydrogenase complex Source: UniProtKB
Keywords - Cellular componenti
Mitochondrion, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 68 | MitochondrionBy similarityAdd BLAST | 68 | |
ChainiPRO_0000020473 | 69 – 454 | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST | 386 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 82 | PhosphoserineCombined sources | 1 | |
Modified residuei | 111 | N6-lipoyllysinePROSITE-ProRule annotation | 1 | |
Modified residuei | 155 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 268 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 273 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 274 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 278 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 308 | N6-acetyllysineCombined sources | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | Q9D2G2 |
jPOSTi | Q9D2G2 |
PaxDbi | Q9D2G2 |
PeptideAtlasi | Q9D2G2 |
PRIDEi | Q9D2G2 |
TopDownProteomicsi | Q9D2G2-1 [Q9D2G2-1] Q9D2G2-2 [Q9D2G2-2] |
2D gel databases
REPRODUCTION-2DPAGEi | Q9D2G2 |
UCD-2DPAGEi | Q9D2G2 |
PTM databases
iPTMneti | Q9D2G2 |
PhosphoSitePlusi | Q9D2G2 |
SwissPalmi | Q9D2G2 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000004789, Expressed in brown adipose tissue and 346 other tissues |
ExpressionAtlasi | Q9D2G2, baseline and differential |
Genevisiblei | Q9D2G2, MM |
Interactioni
Subunit structurei
The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A.
By similarityBinary interactionsi
Q9D2G2
With | #Exp. | IntAct |
---|---|---|
Plec [Q9QXS1] | 2 | EBI-773210,EBI-774583 |
GO - Molecular functioni
- chaperone binding Source: MGI
- heat shock protein binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 219707, 29 interactors |
IntActi | Q9D2G2, 63 interactors |
MINTi | Q9D2G2 |
STRINGi | 10090.ENSMUSP00000060346 |
Miscellaneous databases
RNActi | Q9D2G2, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 71 – 145 | Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST | 75 |
Sequence similaritiesi
Keywords - Domaini
Lipoyl, Transit peptidePhylogenomic databases
eggNOGi | KOG0559, Eukaryota |
GeneTreei | ENSGT00930000151014 |
HOGENOMi | CLU_016733_0_0_1 |
InParanoidi | Q9D2G2 |
OMAi | MKVPSPG |
OrthoDBi | 850255at2759 |
PhylomeDBi | Q9D2G2 |
TreeFami | TF314164 |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit |
InterProi | View protein in InterPro IPR003016, 2-oxoA_DH_lipoyl-BS IPR001078, 2-oxoacid_DH_actylTfrase IPR000089, Biotin_lipoyl IPR023213, CAT-like_dom_sf IPR011053, Single_hybrid_motif IPR006255, SucB |
Pfami | View protein in Pfam PF00198, 2-oxoacid_dh, 1 hit PF00364, Biotin_lipoyl, 1 hit |
SUPFAMi | SSF51230, SSF51230, 1 hit |
TIGRFAMsi | TIGR01347, sucB, 1 hit |
PROSITEi | View protein in PROSITE PS50968, BIOTINYL_LIPOYL, 1 hit PS00189, LIPOYL, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A1Y7VN44 | A0A1Y7VN44_MOUSE | Dihydrolipoyllysine-residue succiny... | Dlst | 59 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 276 | N → S in BAE29011 (PubMed:16141072).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_025015 | 1 – 253 | Missing in isoform 2. 1 PublicationAdd BLAST | 253 | |
Alternative sequenceiVSP_025016 | 254 – 257 | EVDM → MTSL in isoform 2. 1 Publication | 4 |
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 |
CCDSi | CCDS26052.1 [Q9D2G2-1] |
RefSeqi | NP_084501.1, NM_030225.4 [Q9D2G2-1] |
Genome annotation databases
Ensembli | ENSMUST00000053811; ENSMUSP00000060346; ENSMUSG00000004789 [Q9D2G2-1] ENSMUST00000221357; ENSMUSP00000152664; ENSMUSG00000004789 [Q9D2G2-1] |
GeneIDi | 78920 |
KEGGi | mmu:78920 |
UCSCi | uc007ogj.2, mouse [Q9D2G2-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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 |
CCDSi | CCDS26052.1 [Q9D2G2-1] |
RefSeqi | NP_084501.1, NM_030225.4 [Q9D2G2-1] |
3D structure databases
SMRi | Q9D2G2 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 219707, 29 interactors |
IntActi | Q9D2G2, 63 interactors |
MINTi | Q9D2G2 |
STRINGi | 10090.ENSMUSP00000060346 |
Chemistry databases
ChEMBLi | CHEMBL2176822 |
PTM databases
iPTMneti | Q9D2G2 |
PhosphoSitePlusi | Q9D2G2 |
SwissPalmi | Q9D2G2 |
2D gel databases
REPRODUCTION-2DPAGEi | Q9D2G2 |
UCD-2DPAGEi | Q9D2G2 |
Proteomic databases
EPDi | Q9D2G2 |
jPOSTi | Q9D2G2 |
PaxDbi | Q9D2G2 |
PeptideAtlasi | Q9D2G2 |
PRIDEi | Q9D2G2 |
TopDownProteomicsi | Q9D2G2-1 [Q9D2G2-1] Q9D2G2-2 [Q9D2G2-2] |
Protocols and materials databases
Antibodypediai | 45, 193 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000053811; ENSMUSP00000060346; ENSMUSG00000004789 [Q9D2G2-1] ENSMUST00000221357; ENSMUSP00000152664; ENSMUSG00000004789 [Q9D2G2-1] |
GeneIDi | 78920 |
KEGGi | mmu:78920 |
UCSCi | uc007ogj.2, mouse [Q9D2G2-1] |
Organism-specific databases
CTDi | 1743 |
MGIi | MGI:1926170, Dlst |
Phylogenomic databases
eggNOGi | KOG0559, Eukaryota |
GeneTreei | ENSGT00930000151014 |
HOGENOMi | CLU_016733_0_0_1 |
InParanoidi | Q9D2G2 |
OMAi | MKVPSPG |
OrthoDBi | 850255at2759 |
PhylomeDBi | Q9D2G2 |
TreeFami | TF314164 |
Enzyme and pathway databases
UniPathwayi | UPA00223 UPA00868;UER00840 |
Reactomei | R-MMU-389661, Glyoxylate metabolism and glycine degradation R-MMU-71064, Lysine catabolism R-MMU-71403, Citric acid cycle (TCA cycle) |
Miscellaneous databases
BioGRID-ORCSi | 78920, 8 hits in 23 CRISPR screens |
ChiTaRSi | Dlst, mouse |
PROi | PR:Q9D2G2 |
RNActi | Q9D2G2, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000004789, Expressed in brown adipose tissue and 346 other tissues |
ExpressionAtlasi | Q9D2G2, baseline and differential |
Genevisiblei | Q9D2G2, MM |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit |
InterProi | View protein in InterPro IPR003016, 2-oxoA_DH_lipoyl-BS IPR001078, 2-oxoacid_DH_actylTfrase IPR000089, Biotin_lipoyl IPR023213, CAT-like_dom_sf IPR011053, Single_hybrid_motif IPR006255, SucB |
Pfami | View protein in Pfam PF00198, 2-oxoacid_dh, 1 hit PF00364, Biotin_lipoyl, 1 hit |
SUPFAMi | SSF51230, SSF51230, 1 hit |
TIGRFAMsi | TIGR01347, sucB, 1 hit |
PROSITEi | View protein in PROSITE PS50968, BIOTINYL_LIPOYL, 1 hit PS00189, LIPOYL, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ODO2_MOUSE | |
Accessioni | Q9D2G2Primary (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: | December 2, 2020 | |
This is version 163 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families