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Protein

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

Gene

Dlst

Organism
Rattus norvegicus (Rat)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei425 – 4251Sequence Analysis
Active sitei429 – 4291Sequence Analysis

GO - Molecular functioni

  1. chaperone binding Source: RGD
  2. dihydrolipoyllysine-residue succinyltransferase activity Source: RGD
  3. heat shock protein binding Source: RGD

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: RGD
  2. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  3. NADH metabolic process Source: RGD
  4. tricarboxylic acid cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BRENDAi2.3.1.61. 5301.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1359615. Dlst.

Subcellular locationi

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: RGD
  2. mitochondrion Source: RGD
  3. oxoglutarate dehydrogenase complex Source: RGD
  4. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6868Mitochondrion2 PublicationsAdd
BLAST
Chaini69 – 454386Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-lipoyllysinePROSITE-ProRule annotation
Modified residuei155 – 1551N6-acetyllysineBy similarity
Modified residuei268 – 2681N6-acetyllysineBy similarity
Modified residuei273 – 2731N6-acetyllysineBy similarity
Modified residuei274 – 2741N6-acetyllysineBy similarity
Modified residuei278 – 2781N6-acetyllysineBy similarity
Modified residuei308 – 3081N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ01205.
PRIDEiQ01205.

PTM databases

PhosphoSiteiQ01205.

Expressioni

Gene expression databases

GenevestigatoriQ01205.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

IntActiQ01205. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ01205.
SMRiQ01205. Positions 221-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 14575Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiQ01205.
KOiK00658.
PhylomeDBiQ01205.

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.

Q01205-1 [UniParc]FASTAAdd 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131S → M in BAA14397. (PubMed:1918017)Curated
Sequence conflicti52 – 543NSS → TVA in BAA14397. (PubMed:1918017)Curated
Sequence conflicti164 – 1641Y → H in BAA14397. (PubMed:1918017)Curated
Sequence conflicti281 – 2811F → L in BAA14397. (PubMed:1918017)Curated
Sequence conflicti448 – 4481R → A in BAA14397. (PubMed:1918017)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083858 mRNA. Translation: AAH83858.1.
D90401 mRNA. Translation: BAA14397.1.
PIRiA41015.
RefSeqiNP_001006982.2. NM_001006981.2.
UniGeneiRn.99702.

Genome annotation databases

GeneIDi299201.
KEGGirno:299201.
UCSCiRGD:1359615. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083858 mRNA. Translation: AAH83858.1.
D90401 mRNA. Translation: BAA14397.1.
PIRiA41015.
RefSeqiNP_001006982.2. NM_001006981.2.
UniGeneiRn.99702.

3D structure databases

ProteinModelPortaliQ01205.
SMRiQ01205. Positions 221-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ01205. 1 interaction.

PTM databases

PhosphoSiteiQ01205.

Proteomic databases

PaxDbiQ01205.
PRIDEiQ01205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi299201.
KEGGirno:299201.
UCSCiRGD:1359615. rat.

Organism-specific databases

CTDi1743.
RGDi1359615. Dlst.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
HOVERGENiHBG000268.
InParanoidiQ01205.
KOiK00658.
PhylomeDBiQ01205.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
BRENDAi2.3.1.61. 5301.

Miscellaneous databases

NextBioi644993.
PROiQ01205.

Gene expression databases

GenevestigatoriQ01205.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  2. "Purification and molecular cloning of succinyltransferase of the rat alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif of the putative E3 and/or E1 binding site."
    Nakano K., Matuda S., Yamanaka T., Tsubouchi H., Nakagawa S., Titani K., Ohta S., Miyata T.
    J. Biol. Chem. 266:19013-19017(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-454, PROTEIN SEQUENCE OF 69-83.
    Tissue: Heart.
  3. Lubec G., Chen W.-Q., Afjehi-Sadat L., Diao W.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 69-89; 135-145; 262-308 AND 314-326, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.

Entry informationi

Entry nameiODO2_RAT
AccessioniPrimary (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: January 7, 2015
This is version 128 of the entry and version 2 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

External Data

Dasty 3

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 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.