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Protein

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

Gene

DLST

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).1 Publication

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiR-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:2.3.1.61)
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

  • Mitochondrion 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

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

Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002572.

Structurei

3D structure databases

ProteinModelPortaliQ9N0F1.
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
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0559. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133844.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiQ9N0F1.
KOiK00658.
OMAiEGKKDMK.
OrthoDBiEOG091G08FX.
TreeFamiTF314164.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ9N0F1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000002572.

Proteomic databases

PaxDbiQ9N0F1.
PeptideAtlasiQ9N0F1.
PRIDEiQ9N0F1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000002639; ENSSSCP00000002572; ENSSSCG00000002374.
GeneIDi397690.
KEGGissc:397690.

Organism-specific databases

CTDi1743.

Phylogenomic databases

eggNOGiKOG0559. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133844.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiQ9N0F1.
KOiK00658.
OMAiEGKKDMK.
OrthoDBiEOG091G08FX.
TreeFamiTF314164.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
ReactomeiR-SSC-71064. Lysine catabolism.
R-SSC-71403. Citric acid cycle (TCA cycle).

Gene expression databases

BgeeiENSSSCG00000002374.
GenevisibleiQ9N0F1. SS.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODO2_PIG
AccessioniPrimary (citable) accession number: Q9N0F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 110 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.