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Protein

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

Gene

DLST

Organism
Bos taurus (Bovine)
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)-lipoate1 PublicationNote: Binds 1 lipoyl cofactor covalently.1 Publication

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 sitei426Sequence analysis1
Active sitei430Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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 – 68MitochondrionBy similarityAdd BLAST68
ChainiPRO_000016225269 – 455Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST387

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei82PhosphoserineBy similarity1
Modified residuei111N6-lipoyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei155N6-acetyllysineBy similarity1
Modified residuei269N6-acetyllysineBy similarity1
Modified residuei274N6-acetyllysineBy similarity1
Modified residuei275N6-acetyllysineBy similarity1
Modified residuei279N6-acetyllysineBy similarity1
Modified residuei309N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiP11179
PRIDEiP11179

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

Protein-protein interaction databases

IntActiP11179, 1 interactor

Structurei

3D structure databases

ProteinModelPortaliP11179
SMRiP11179
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

HOGENOMiHOG000281563
HOVERGENiHBG000268
InParanoidiP11179
KOiK00658

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.

P11179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRSRCASR AFSRSLSAFQ KGNCPLVRRS LPGISLCQGP GYPDSRKTVI
60 70 80 90 100
NSSNIFSVRF FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE
110 120 130 140 150
DEVVCEIETD KTSVQVPSPA NGVIEALLVP DGGKVEGGTP LFTLRKTGAA
160 170 180 190 200
PAKAKPAAAP AAAAPKAEPT VSAVPPPPAA PIPTQMPPVP SPSQPLTSKP
210 220 230 240 250
VSAVKPTAAP PRAEAGAGVG LRSEHREKMN RMRQRIAQRL KEAQNTCAML
260 270 280 290 300
TTFNEIDMSN IQEMRARHKD AFLKKHNLKL GFMSAFVKAS AFALQEQPVV
310 320 330 340 350
NAVIDDATKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS
360 370 380 390 400
ELGEKARKNE LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA
410 420 430 440 450
IVDRPVVIGG KVEVRPMMYV ALTYDHRLID GREAVTFLRK IKAAVEDPRV

LLLDL
Length:455
Mass (Da):48,973
Last modified:October 17, 2006 - v2
Checksum:iDB2124A4D06C389B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT026207 mRNA Translation: ABG67046.1
PIRiS00123
RefSeqiNP_001068750.1, NM_001075282.1
UniGeneiBt.41191

Genome annotation databases

GeneIDi506888
KEGGibta:506888

Similar proteinsi

Entry informationi

Entry nameiODO2_BOVIN
AccessioniPrimary (citable) accession number: P11179
Secondary accession number(s): Q0V8L1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 17, 2006
Last modified: April 25, 2018
This is version 120 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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