Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

DLST

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex (PubMed:10806400). The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2 (PubMed:10806400). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). 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 similarity1 Publication

Catalytic activityi

Succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine.1 Publication

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. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  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

  • dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiR-SSC-389661 Glyoxylate metabolism and glycine degradation
R-SSC-71064 Lysine catabolism
R-SSC-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:2.3.1.611 Publication)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
E2K
E2o
Short name:
PE2o
Gene namesi
Name:DLST
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 7

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi374S → A: Loss of activity. 1 Publication1
Mutagenesisi426H → C: 16% of activity. 1 Publication1
Mutagenesisi430D → A, E or N: Loss of activity. 1 Publication1
Mutagenesisi451 – 453LLL → AAA or DDD: Loss of activity. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 68MitochondrionAdd BLAST68
ChainiPRO_000002047469 – 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
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

PaxDbiQ9N0F1
PeptideAtlasiQ9N0F1
PRIDEiQ9N0F1

Expressioni

Gene expression databases

BgeeiENSSSCG00000002374
GenevisibleiQ9N0F1 SS

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

STRINGi9823.ENSSSCP00000002572

Structurei

3D structure databases

ProteinModelPortaliQ9N0F1
SMRiQ9N0F1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni221 – 453CatalyticAdd BLAST233

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi151 – 215Pro-richAdd BLAST65

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0559 Eukaryota
COG0508 LUCA
GeneTreeiENSGT00920000149063
HOGENOMiHOG000281563
HOVERGENiHBG000268
InParanoidiQ9N0F1
KOiK00658
OMAiMKVPSPG
OrthoDBiEOG091G08FX
TreeFamiTF314164

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.

Q9N0F1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGISLCQGP GYPDSRKIVI
60 70 80 90 100
SNSSVLNVRF FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE
110 120 130 140 150
DEVVCEIETD KTSVQVPSPA NGVIEALLVP DGGKVEGGTP LFTLRKTGAA
160 170 180 190 200
PAKAKPAEAP AAAAPKAEPA VSAVPPPPAA SIPTQMPPVP SPPQPLTSKP
210 220 230 240 250
VSAVKPTAAP PVAEPGAVKG LRAEHREKMN RMRQRIAQRL KEAQNTCAML
260 270 280 290 300
TTFNEIDMSN IQDMRARHKE AFLKKHNLKL GFMSAFVKAS AFALQEQPVV
310 320 330 340 350
NAVIDDTTKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS
360 370 380 390 400
ELGEKARKNE LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA
410 420 430 440 450
IVDRPVAVGG KVEIRPMMYV ALTYDHRLID GREAVTFLRK IKAAVEDPRV

LLLDL
Length:455
Mass (Da):48,977
Last modified:October 1, 2000 - v1
Checksum:i563B5E7455C842FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035206 mRNA Translation: BAA95700.1
RefSeqiNP_999562.1, NM_214397.1
UniGeneiSsc.2730

Genome annotation databases

EnsembliENSSSCT00000002639; ENSSSCP00000002572; ENSSSCG00000002374
GeneIDi397690
KEGGissc:397690

Similar proteinsi

Entry informationi

Entry nameiODO2_PIG
AccessioniPrimary (citable) accession number: Q9N0F1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: June 20, 2018
This is version 119 of the entry and version 1 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health