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Protein

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

Gene

DLST

Organism
Homo sapiens (Human)
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).

Catalytic activityi

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

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

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 sitei424Sequence analysis1
Active sitei428Sequence 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

BioCyciMetaCyc:HS04324-MONOMER.
ZFISH:HS04324-MONOMER.
ReactomeiR-HSA-389661. Glyoxylate metabolism and glycine degradation.
R-HSA-71064. Lysine catabolism.
R-HSA-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
Gene namesi
Name:DLST
Synonyms:DLTS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:2911. DLST.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
  • oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

DisGeNETi1743.
OpenTargetsiENSG00000119689.
PharmGKBiPA27367.

Polymorphism and mutation databases

BioMutaiDLST.
DMDMi317373578.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 67Mitochondrion1 PublicationAdd BLAST67
ChainiPRO_000002047268 – 453Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST386

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei81PhosphoserineBy similarity1
Modified residuei110N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei154N6-acetyllysineBy similarity1
Modified residuei267N6-acetyllysineBy similarity1
Modified residuei272N6-acetyllysineBy similarity1
Modified residuei273N6-acetyllysineBy similarity1
Modified residuei277N6-acetyllysineBy similarity1
Modified residuei307N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP36957.
MaxQBiP36957.
PaxDbiP36957.
PeptideAtlasiP36957.
PRIDEiP36957.
TopDownProteomicsiP36957-1. [P36957-1]

2D gel databases

OGPiP36957.
UCD-2DPAGEP36957.

PTM databases

iPTMnetiP36957.
PhosphoSitePlusiP36957.
SwissPalmiP36957.

Expressioni

Gene expression databases

BgeeiENSG00000119689.
CleanExiHS_DLST.
ExpressionAtlasiP36957. baseline and differential.
GenevisibleiP36957. HS.

Organism-specific databases

HPAiHPA003010.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

BioGridi108087. 32 interactors.
IntActiP36957. 27 interactors.
MINTiMINT-3014449.
STRINGi9606.ENSP00000335304.

Structurei

3D structure databases

ProteinModelPortaliP36957.
SMRiP36957.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini70 – 144Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST75

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.
InParanoidiP36957.
KOiK00658.
OMAiEGKKDMK.
OrthoDBiEOG091G08FX.
PhylomeDBiP36957.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P36957-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPNSRKVVI
60 70 80 90 100
NNSVFSVRFF RTTAVCKDDL VTVKTPAFAE SVTEGDVRWE KAVGDTVAED
110 120 130 140 150
EVVCEIETDK TSVQVPSPAN GVIEALLVPD GGKVEGGTPL FTLRKTGAAP
160 170 180 190 200
AKAKPAEAPA AAAPKAEPTA AAVPPPAAPI PTQMPPVPSP SQPPSGKPVS
210 220 230 240 250
AVKPTVAPPL AEPGAGKGLR SEHREKMNRM RQRIAQRLKE AQNTCAMLTT
260 270 280 290 300
FNEIDMSNIQ EMRARHKEAF LKKHNLKLGF MSAFVKASAF ALQEQPVVNA
310 320 330 340 350
VIDDTTKEVV YRDYIDISVA VATPRGLVVP VIRNVEAMNF ADIERTITEL
360 370 380 390 400
GEKARKNELA IEDMDGGTFT ISNGGVFGSL FGTPIINPPQ SAILGMHGIF
410 420 430 440 450
DRPVAIGGKV EVRPMMYVAL TYDHRLIDGR EAVTFLRKIK AAVEDPRVLL

LDL
Length:453
Mass (Da):48,755
Last modified:January 11, 2011 - v4
Checksum:iA30E8CC959106B8F
GO
Isoform 2 (identifier: P36957-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MLSRSRCVSRAFSRSLSAFQKGN → MTWLQSKPQRLQNLSQREMSGGR
     24-109: Missing.

Note: No experimental confirmation available.
Show »
Length:367
Mass (Da):39,553
Checksum:i3EEF7F48175530EC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 15RS → AP in BAA03871 (PubMed:8268217).Curated2
Sequence conflicti14 – 15RS → AP in BAA05536 (PubMed:8076640).Curated2
Sequence conflicti14 – 15RS → AP in AAB59629 (Ref. 3) Curated2
Sequence conflicti132G → T in BAA03871 (PubMed:8268217).Curated1
Sequence conflicti212E → D in BAA03871 (PubMed:8268217).Curated1
Sequence conflicti212E → D in BAA05536 (PubMed:8076640).Curated1
Sequence conflicti312R → T in BAA05536 (PubMed:8076640).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004976213P → A.2 PublicationsCorresponds to variant rs2853769dbSNPEnsembl.1
Natural variantiVAR_004977384P → T.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0564391 – 23MLSRS…FQKGN → MTWLQSKPQRLQNLSQREMS GGR in isoform 2. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_05644024 – 109Missing in isoform 2. 1 PublicationAdd BLAST86

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16373 mRNA. Translation: BAA03871.1.
D26535 Genomic DNA. Translation: BAA05536.1.
L37418 mRNA. Translation: AAB59629.1.
AK289414 mRNA. Translation: BAF82103.1.
AK299505 mRNA. Translation: BAH13054.1.
AC006530 Genomic DNA. Translation: AAD30181.1.
CH471061 Genomic DNA. Translation: EAW81199.1.
BC000302 mRNA. Translation: AAH00302.1.
BC001922 mRNA. Translation: AAH01922.1.
CCDSiCCDS9833.1. [P36957-1]
PIRiS39786. PN0673.
RefSeqiNP_001924.2. NM_001933.4. [P36957-1]
UniGeneiHs.525459.

Genome annotation databases

EnsembliENST00000334220; ENSP00000335304; ENSG00000119689. [P36957-1]
GeneIDi1743.
KEGGihsa:1743.
UCSCiuc001xqv.3. human. [P36957-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16373 mRNA. Translation: BAA03871.1.
D26535 Genomic DNA. Translation: BAA05536.1.
L37418 mRNA. Translation: AAB59629.1.
AK289414 mRNA. Translation: BAF82103.1.
AK299505 mRNA. Translation: BAH13054.1.
AC006530 Genomic DNA. Translation: AAD30181.1.
CH471061 Genomic DNA. Translation: EAW81199.1.
BC000302 mRNA. Translation: AAH00302.1.
BC001922 mRNA. Translation: AAH01922.1.
CCDSiCCDS9833.1. [P36957-1]
PIRiS39786. PN0673.
RefSeqiNP_001924.2. NM_001933.4. [P36957-1]
UniGeneiHs.525459.

3D structure databases

ProteinModelPortaliP36957.
SMRiP36957.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108087. 32 interactors.
IntActiP36957. 27 interactors.
MINTiMINT-3014449.
STRINGi9606.ENSP00000335304.

PTM databases

iPTMnetiP36957.
PhosphoSitePlusiP36957.
SwissPalmiP36957.

Polymorphism and mutation databases

BioMutaiDLST.
DMDMi317373578.

2D gel databases

OGPiP36957.
UCD-2DPAGEP36957.

Proteomic databases

EPDiP36957.
MaxQBiP36957.
PaxDbiP36957.
PeptideAtlasiP36957.
PRIDEiP36957.
TopDownProteomicsiP36957-1. [P36957-1]

Protocols and materials databases

DNASUi1743.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334220; ENSP00000335304; ENSG00000119689. [P36957-1]
GeneIDi1743.
KEGGihsa:1743.
UCSCiuc001xqv.3. human. [P36957-1]

Organism-specific databases

CTDi1743.
DisGeNETi1743.
GeneCardsiDLST.
H-InvDBHIX0131240.
HGNCiHGNC:2911. DLST.
HPAiHPA003010.
MIMi126063. gene.
neXtProtiNX_P36957.
OpenTargetsiENSG00000119689.
PharmGKBiPA27367.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0559. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133844.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiP36957.
KOiK00658.
OMAiEGKKDMK.
OrthoDBiEOG091G08FX.
PhylomeDBiP36957.
TreeFamiTF314164.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
BioCyciMetaCyc:HS04324-MONOMER.
ZFISH:HS04324-MONOMER.
ReactomeiR-HSA-389661. Glyoxylate metabolism and glycine degradation.
R-HSA-71064. Lysine catabolism.
R-HSA-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiDLST. human.
GeneWikiiDLST.
GenomeRNAii1743.
PROiP36957.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119689.
CleanExiHS_DLST.
ExpressionAtlasiP36957. baseline and differential.
GenevisibleiP36957. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P36957
Secondary accession number(s): B7Z5W8
, E7ESY5, Q7LDY7, Q9BQ32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 184 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.