FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). 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 N⁶-(dihydrolipoyl)lysine = CoA + enzyme N⁶-(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: Forms a 24-polypeptide structural core with octahedral symmetry (By similarity).
SUBCELLULAR LOCATION: Mitochondrion (By similarity).
SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
SIMILARITY: Contains 1 lipoyl-binding domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U40758; AAC59779.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P07016; 1C4T. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q90512.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0045252;	Cellular component: oxoglutarate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004149;	Molecular function: dihydrolipoyllysine-residue succinyltransferase activity (inferred from electronic annotation from InterPro).
GO:0031405;	Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR000089; Biotin_lipoyl.
IPR006255; SucB.
Graphical view of domain structure.

Pfam

PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 1.
Pfam graphical view of domain structure.

ProDom

PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01347; sucB; 1.

PROSITE

PS50968; BIOTINYL_LIPOYL; 1.
PS00189; LIPOYL; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q90512.

Genome annotation databases

Ensembl

NEWSINFRUG00000132417; Fugu rubripes. [Contig view]

Phylogenomic databases

HOVERGEN

Q90512; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Lipoyl; Mitochondrion; Transferase; Transit peptide; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 36`	`>36`	`Mitochondrion (By similarity).`
`CHAIN`	`37 409`	`373`	`Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial.`	`PRO_0000020476`
`DOMAIN`	`40 112`	`73`	`Lipoyl-binding.`
`COMPBIAS`	`133 139`	`7`	`Poly-Pro.`
`ACT_SITE`	`380 380`		`Potential.`
`ACT_SITE`	`384 384`		`Potential.`
`BINDING`	`79 79`		`Lipoyl (covalent) (Potential).`
`NON_TER`	`1 1`

Sequence information

Length: 409 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 44112 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 5A429FD99DA43873 [This is a checksum on the sequence]

        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

Q90512 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools