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

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Q90512 (ODO2_TAKRU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

dlst

Organism

Takifugu rubripes (Japanese pufferfish) (Fugu rubripes) [Reference proteome]

Taxonomic identifier

31033 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Tetraodontiformes › Tetradontoidea › Tetraodontidae › Takifugu

Protein attributes

Sequence length	409 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO₂. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Lipoyl Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

‹1 – 36

›36

Mitochondrion By similarity

Chain

37 – 409

373

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

PRO_0000020476

Regions

Domain

40 – 112

Lipoyl-binding

Compositional bias

133 – 139

Poly-Pro

Sites

Active site

380

Potential

Active site

384

Potential

Amino acid modifications

Modified residue

N6-lipoyllysine Potential

Experimental info

Non-terminal residue

Sequences

Sequence

Length

Mass (Da)

Tools

Q90512 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5A429FD99DA43873
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FASTA

409

44,112

        10         20         30         40         50         60 
SSVCRRLIFR TSRPGERASS QNSFHVRYFR TSVVHRDDLV TVKTPAFAES VTEGDVRWEK 

        70         80         90        100        110        120 
AVGDSVTEDE VVCEIETDKT SVQVPSPAAG VIEELLVPDG GKVEGGTPLF KLRKGAAAEA 

       130        140        150        160        170        180 
APSSVTEPVT AAPPPPPPPV SAPTAMPSVP PVPTQALQAK PVPAPTLPEP STLGGRGESR 

       190        200        210        220        230        240 
VKMSRMRLRI AQRLKEAQNT CAMLTTFNEV DMSNIQEMRT LHKDAFLKKH SIKLGFMSAF 

       250        260        270        280        290        300 
VKAAAHALTD QPAVNAVIDG ATNEIVYRDY VDISVAVATP KGLVVPVIRN VETMNFADIE 

       310        320        330        340        350        360 
RTINALGEKA RNNELAVEDM DGGTFTISNG GVFGSLFGTP IINPPQSAIL GMHGIFQRPV 

       370        380        390        400 
AVDGKAEIRP MMYVALTYDH RLVDGREAVT FLRKIKAAVE DPRALLLDM

« Hide

References

[1]

"Conservation of synteny between the genome of the pufferfish (Fugu rubripes) and the region on human chromosome 14 (14q24.3) associated with familial Alzheimer disease (AD3 locus)."
Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J., Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.
Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U40758 Genomic DNA. Translation: AAC59779.1.
3D structure databases
ProteinModelPortal	Q90512.
SMR	Q90512. Positions 180-406.
ModBase	Search...
Protein-protein interaction databases
STRING	31033.ENSTRUP00000025327.
Proteomic databases
PRIDE	Q90512.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG0508.
Enzyme and pathway databases
UniPathway	UPA00868; UER00840.
Family and domain databases
Gene3D	3.30.559.10. 1 hit.
InterPro	IPR003016. 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]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_TAKRU

Accession

Primary (citable) accession number: Q90512

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents