Dlst

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:

Alpha-aminoadipic semialdehyde synthase, mitochondrial (Aass)
Alpha-aminoadipic semialdehyde synthase, mitochondrial (Aass)
no protein annotated in this organism
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Aadat)
no protein annotated in this organism
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 key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	425	Sequence analysis		1
Active siteⁱ	429	Sequence analysis		1

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

2-oxoglutarate metabolic process
Source: RGD
Inferred from direct assayⁱ
- 3571202
histone succinylation Source: UniProtKB
L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
NADH metabolic process
Source: RGD
Inferred from direct assayⁱ
- 9405249
succinyl-CoA metabolic process Source: UniProtKB
tricarboxylic acid cycle
Source: RGD
Inferred by curatorⁱ
- 9405249

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Biological process	Tricarboxylic acid cycle

Enzyme and pathway databases

BRENDAⁱ	2.3.1.61 5301
UniPathwayⁱ	UPA00868; 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
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	1359615 Dlst

RGDⁱ

1359615 Dlst

Keywords - Cellular componentⁱ

Mitochondrion, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 68	Mitochondrion2 PublicationsAdd BLAST		68
ChainⁱPRO_0000020475	69 – 454	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST		386

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	82	PhosphoserineBy similarity	1
Modified residueⁱ	111	N6-lipoyllysinePROSITE-ProRule annotation	1
Modified residueⁱ	155	N6-acetyllysineBy similarity	1
Modified residueⁱ	268	N6-acetyllysineBy similarity	1
Modified residueⁱ	273	N6-acetyllysineBy similarity	1
Modified residueⁱ	274	N6-acetyllysineBy similarity	1
Modified residueⁱ	278	N6-acetyllysineBy similarity	1
Modified residueⁱ	308	N6-acetyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

PaxDbⁱ	Q01205
PRIDEⁱ	Q01205

PTM databases

iPTMnetⁱ	Q01205
PhosphoSitePlusⁱ	Q01205

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
Inferred from physical interactionⁱ
- 9811814
heat shock protein binding
Source: RGD
Inferred from physical interactionⁱ
- 9811814

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

IntActⁱ	Q01205, 1 interactor
STRINGⁱ	10116.ENSRNOP00000007298

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q01205
SMRⁱ	Q01205
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	71 – 145	Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST		75

Sequence similaritiesⁱ

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domainⁱ

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG0559 Eukaryota COG0508 LUCA
HOGENOMⁱ	HOG000281563
HOVERGENⁱ	HBG000268
InParanoidⁱ	Q01205
KEGG Orthology (KO) More...KOⁱ	K00658
PhylomeDBⁱ	Q01205

Family and domain databases

Gene3Dⁱ	3.30.559.10, 1 hit
InterProⁱ	View 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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00198 2-oxoacid_dh, 1 hit PF00364 Biotin_lipoyl, 1 hit
SUPFAMⁱ	SSF51230 SSF51230, 1 hit
TIGRFAMsⁱ	TIGR01347 sucB, 1 hit
PROSITEⁱ	View 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]FASTA Add 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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	13	S → M in BAA14397 (PubMed:1918017).Curated	1
Sequence conflictⁱ	52 – 54	NSS → TVA in BAA14397 (PubMed:1918017).Curated	3
Sequence conflictⁱ	164	Y → H in BAA14397 (PubMed:1918017).Curated	1
Sequence conflictⁱ	281	F → L in BAA14397 (PubMed:1918017).Curated	1
Sequence conflictⁱ	448	R → A in BAA14397 (PubMed:1918017).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BC083858 mRNA Translation: AAH83858.1 D90401 mRNA Translation: BAA14397.1
PIRⁱ	A41015
NCBI Reference Sequences More...RefSeqⁱ	NP_001006982.2, NM_001006981.2
UniGeneⁱ	Rn.99702

Genome annotation databases

GeneIDⁱ	299201
KEGGⁱ	rno:299201
UCSC genome browser More...UCSCⁱ	RGD:1359615 rat

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
Q01205	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		HUMAN		453
DLST isoform 2		PANTR		453
UPI000C811474		LOXAF		467
UPI0003C00A6F		wild yak		462
dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		DIPOR		458
+116

Protein	Similar proteins		Species	Score	Length
Q01205	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		HUMAN		453
DLST isoform 2		PANTR		453
UPI000C811474		LOXAF		467
UPI0003C00A6F		wild yak		462
dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		DIPOR		458
+264

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BC083858 mRNA Translation: AAH83858.1 D90401 mRNA Translation: BAA14397.1
PIRⁱ	A41015
NCBI Reference Sequences More...RefSeqⁱ	NP_001006982.2, NM_001006981.2
UniGeneⁱ	Rn.99702

3D structure databases

ProteinModelPortalⁱ	Q01205
SMRⁱ	Q01205
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	Q01205, 1 interactor
STRINGⁱ	10116.ENSRNOP00000007298

PTM databases

iPTMnetⁱ	Q01205
PhosphoSitePlusⁱ	Q01205

Proteomic databases

PaxDbⁱ	Q01205
PRIDEⁱ	Q01205

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	299201
KEGGⁱ	rno:299201
UCSC genome browser More...UCSCⁱ	RGD:1359615 rat

Organism-specific databases

CTDⁱ	1743
Rat genome database More...RGDⁱ	1359615 Dlst

Phylogenomic databases

eggNOGⁱ	KOG0559 Eukaryota COG0508 LUCA
HOGENOMⁱ	HOG000281563
HOVERGENⁱ	HBG000268
InParanoidⁱ	Q01205
KEGG Orthology (KO) More...KOⁱ	K00658
PhylomeDBⁱ	Q01205

Enzyme and pathway databases

UniPathwayⁱ	UPA00868; UER00840
BRENDAⁱ	2.3.1.61 5301

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q01205

PROⁱ

PR:Q01205

Family and domain databases

Gene3Dⁱ	3.30.559.10, 1 hit
InterProⁱ	View 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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00198 2-oxoacid_dh, 1 hit PF00364 Biotin_lipoyl, 1 hit
SUPFAMⁱ	SSF51230 SSF51230, 1 hit
TIGRFAMsⁱ	TIGR01347 sucB, 1 hit
PROSITEⁱ	View protein in PROSITE PS50968 BIOTINYL_LIPOYL, 1 hit PS00189 LIPOYL, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ODO2_RAT
Accessionⁱ	Q01205Primary (citable) accession number: Q01205 Secondary accession number(s): Q5XI35
Entry historyⁱ	Integrated 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 statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

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Proteomes

Annotation systems

Supporting data

UniProtKB - Q01205 (ODO2_RAT)

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

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine degradation via saccharopine pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Nucleus

Mitochondrion

Nucleus

Plasma Membrane

Other locations

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Pathwayⁱ: L-lysine degradation via saccharopine pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ