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Protein

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

Gene

dlst

Organism
Takifugu rubripes (Japanese pufferfish) (Fugu rubripes)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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:
  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 sitei380Sequence analysis1
Active sitei384Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00868; 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
OrganismiTakifugu rubripes (Japanese pufferfish) (Fugu rubripes)
Taxonomic identifieri31033 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaTetraodontiformesTetradontoideaTetraodontidaeTakifugu
Proteomesi
  • UP000005226 Componenti: Unplaced

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei‹1 – 36MitochondrionBy similarityAdd BLAST›36
ChainiPRO_000002047637 – 409Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialAdd BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79N6-lipoyllysinePROSITE-ProRule annotation1

Proteomic databases

PRIDEiQ90512

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

Structurei

3D structure databases

ProteinModelPortaliQ90512
SMRiQ90512
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 113Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST75

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi133 – 139Poly-Pro7

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

InParanoidiQ90512

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: Fragment.

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

Q90512-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SSVCRRLIFR TSRPGERASS QNSFHVRYFR TSVVHRDDLV TVKTPAFAES
60 70 80 90 100
VTEGDVRWEK AVGDSVTEDE VVCEIETDKT SVQVPSPAAG VIEELLVPDG
110 120 130 140 150
GKVEGGTPLF KLRKGAAAEA APSSVTEPVT AAPPPPPPPV SAPTAMPSVP
160 170 180 190 200
PVPTQALQAK PVPAPTLPEP STLGGRGESR VKMSRMRLRI AQRLKEAQNT
210 220 230 240 250
CAMLTTFNEV DMSNIQEMRT LHKDAFLKKH SIKLGFMSAF VKAAAHALTD
260 270 280 290 300
QPAVNAVIDG ATNEIVYRDY VDISVAVATP KGLVVPVIRN VETMNFADIE
310 320 330 340 350
RTINALGEKA RNNELAVEDM DGGTFTISNG GVFGSLFGTP IINPPQSAIL
360 370 380 390 400
GMHGIFQRPV AVDGKAEIRP MMYVALTYDH RLVDGREAVT FLRKIKAAVE

DPRALLLDM
Length:409
Mass (Da):44,112
Last modified:November 1, 1996 - v1
Checksum:i5A429FD99DA43873
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40758 Genomic DNA Translation: AAC59779.1

Similar proteinsi

Entry informationi

Entry nameiODO2_TAKRU
AccessioniPrimary (citable) accession number: Q90512
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 25, 2018
This is version 108 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, Reference proteome
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Main funding by: National Institutes of Health