UniProtKB - Q01205 (ODO2_RAT)
Protein
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Gene
Dlst
Organism
Rattus norvegicus (Rat)
Status
Functioni
Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2 (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity).By similarity
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
(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity
: 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), Alpha-aminoadipic semialdehyde synthase, mitochondrial (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), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial, 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: RGD
- dihydrolipoyllysine-residue succinyltransferase activity Source: RGD
- heat shock protein binding Source: RGD
- transferase activity, transferring acyl groups Source: RGD
GO - Biological processi
- 2-oxoglutarate metabolic process Source: RGD
- histone succinylation Source: UniProtKB
- L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
- NADH metabolic process Source: RGD
- 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
BRENDAi | 2.3.1.61, 5301 |
Reactomei | R-RNO-389661, Glyoxylate metabolism and glycine degradation R-RNO-71064, Lysine catabolism R-RNO-71403, Citric acid cycle (TCA cycle) |
SABIO-RKi | Q01205 |
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 | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 1359615, 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: RGD
Nucleus
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: RGD
Other locations
- intracellular membrane-bounded organelle Source: RGD
- oxoglutarate dehydrogenase complex Source: RGD
Keywords - Cellular componenti
Mitochondrion, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 68 | Mitochondrion2 PublicationsAdd BLAST | 68 | |
ChainiPRO_0000020475 | 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 | PhosphoserineBy similarity | 1 | |
Modified residuei | 111 | N6-lipoyllysinePROSITE-ProRule annotation | 1 | |
Modified residuei | 155 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 268 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 273 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 274 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 278 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 308 | N6-acetyllysineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
jPOSTi | Q01205 |
PaxDbi | Q01205 |
PRIDEi | Q01205 |
PTM databases
iPTMneti | Q01205 |
PhosphoSitePlusi | Q01205 |
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 similarityGO - Molecular functioni
- chaperone binding Source: RGD
- heat shock protein binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 256153, 2 interactors |
IntActi | Q01205, 1 interactor |
STRINGi | 10116.ENSRNOP00000007298 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 71 – 145 | Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST | 75 |
Sequence similaritiesi
Belongs to the 2-oxoacid dehydrogenase family.Curated
Keywords - Domaini
Lipoyl, Transit peptidePhylogenomic databases
eggNOGi | KOG0559, Eukaryota |
InParanoidi | Q01205 |
OrthoDBi | 850255at2759 |
PhylomeDBi | Q01205 |
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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
Q01205-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPDSRKMVI
60 70 80 90 100
NNSSVFSVRF FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE
110 120 130 140 150
DEVVCEIETD KTSVQVPSPA NGIIEALLVP DGGKVEGGTP LFTLRKTGAA
160 170 180 190 200
PAKAKPAEAP ATAYKAAPEA PAAPPPPVAP VPTQMPPVPS 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 QSAILGMHGI
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 basketG3V6P2 | G3V6P2_RAT | Dihydrolipoyllysine-residue succiny... | Dlst rCG_21026 | 454 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 13 | S → M in BAA14397 (PubMed:1918017).Curated | 1 | |
Sequence conflicti | 52 – 54 | NSS → TVA in BAA14397 (PubMed:1918017).Curated | 3 | |
Sequence conflicti | 164 | Y → H in BAA14397 (PubMed:1918017).Curated | 1 | |
Sequence conflicti | 281 | F → L in BAA14397 (PubMed:1918017).Curated | 1 | |
Sequence conflicti | 448 | R → A in BAA14397 (PubMed:1918017).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC083858 mRNA Translation: AAH83858.1 D90401 mRNA Translation: BAA14397.1 |
PIRi | A41015 |
RefSeqi | NP_001006982.2, NM_001006981.2 |
Genome annotation databases
GeneIDi | 299201 |
KEGGi | rno:299201 |
UCSCi | RGD:1359615, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC083858 mRNA Translation: AAH83858.1 D90401 mRNA Translation: BAA14397.1 |
PIRi | A41015 |
RefSeqi | NP_001006982.2, NM_001006981.2 |
3D structure databases
SMRi | Q01205 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 256153, 2 interactors |
IntActi | Q01205, 1 interactor |
STRINGi | 10116.ENSRNOP00000007298 |
PTM databases
iPTMneti | Q01205 |
PhosphoSitePlusi | Q01205 |
Proteomic databases
jPOSTi | Q01205 |
PaxDbi | Q01205 |
PRIDEi | Q01205 |
Genome annotation databases
GeneIDi | 299201 |
KEGGi | rno:299201 |
UCSCi | RGD:1359615, rat |
Organism-specific databases
CTDi | 1743 |
RGDi | 1359615, Dlst |
Phylogenomic databases
eggNOGi | KOG0559, Eukaryota |
InParanoidi | Q01205 |
OrthoDBi | 850255at2759 |
PhylomeDBi | Q01205 |
Enzyme and pathway databases
UniPathwayi | UPA00223 UPA00868;UER00840 |
BRENDAi | 2.3.1.61, 5301 |
Reactomei | R-RNO-389661, Glyoxylate metabolism and glycine degradation R-RNO-71064, Lysine catabolism R-RNO-71403, Citric acid cycle (TCA cycle) |
SABIO-RKi | Q01205 |
Miscellaneous databases
PROi | PR:Q01205 |
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_RAT | |
Accessioni | Q01205Primary (citable) accession number: Q01205 Secondary accession number(s): Q5XI35 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1993 |
Last sequence update: | April 12, 2005 | |
Last modified: | December 2, 2020 | |
This is version 158 of the entry and version 2 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
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families