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Protein

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

Gene

Dlst

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(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.
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

  • chaperone binding Source: RGD
  • dihydrolipoyllysine-residue succinyltransferase activity Source: RGD
  • heat shock protein binding 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: RGD

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BRENDAi2.3.1.61 5301
UniPathwayiUPA00868; 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1359615 Dlst

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 68Mitochondrion2 PublicationsAdd BLAST68
ChainiPRO_000002047569 – 454Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST386

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei82PhosphoserineBy similarity1
Modified residuei111N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei155N6-acetyllysineBy similarity1
Modified residuei268N6-acetyllysineBy similarity1
Modified residuei273N6-acetyllysineBy similarity1
Modified residuei274N6-acetyllysineBy similarity1
Modified residuei278N6-acetyllysineBy similarity1
Modified residuei308N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ01205
PRIDEiQ01205

PTM databases

iPTMnetiQ01205
PhosphoSitePlusiQ01205

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 similarity

GO - Molecular functioni

  • chaperone binding Source: RGD
  • heat shock protein binding Source: RGD

Protein-protein interaction databases

IntActiQ01205, 1 interactor
STRINGi10116.ENSRNOP00000007298

Structurei

3D structure databases

ProteinModelPortaliQ01205
SMRiQ01205
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

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0559 Eukaryota
COG0508 LUCA
HOGENOMiHOG000281563
HOVERGENiHBG000268
InParanoidiQ01205
KOiK00658
PhylomeDBiQ01205

Family and domain databases

Gene3Di3.30.559.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
TIGRFAMsiTIGR01347 sucB, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q01205-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:454
Mass (Da):48,925
Last modified:April 12, 2005 - v2
Checksum:i2818F530F4B7C683
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13S → M in BAA14397 (PubMed:1918017).Curated1
Sequence conflicti52 – 54NSS → TVA in BAA14397 (PubMed:1918017).Curated3
Sequence conflicti164Y → H in BAA14397 (PubMed:1918017).Curated1
Sequence conflicti281F → L in BAA14397 (PubMed:1918017).Curated1
Sequence conflicti448R → A in BAA14397 (PubMed:1918017).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083858 mRNA Translation: AAH83858.1
D90401 mRNA Translation: BAA14397.1
PIRiA41015
RefSeqiNP_001006982.2, NM_001006981.2
UniGeneiRn.99702

Genome annotation databases

GeneIDi299201
KEGGirno:299201
UCSCiRGD:1359615 rat

Similar proteinsi

Entry informationi

Entry nameiODO2_RAT
AccessioniPrimary (citable) accession number: Q01205
Secondary accession number(s): Q5XI35
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 12, 2005
Last modified: June 20, 2018
This is version 146 of the entry and version 2 of the sequence. See 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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