NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).

Comments

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).
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

BA000003; BAB13012.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_240126.1; -.

3D structure databases

HSSP

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

ModBase

P57389.

Enzyme and pathway databases

BioCyc

BSP107806:BU303-MON; -.

Ontologies

GO:0031405;	Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
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; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1110002; -.

GenomeReviews

BA000003_GR; BU303.

KEGG

buc:BU303; -.

Phylogenomic databases

HOGENOM

P57389; -.

Genome annotation databases

CMR

P57389; BU303.

Other

UniRef

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

Keywords

Acyltransferase; Complete proteome; Lipoyl; Transferase; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 420`	`420`	`Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex.`	`PRO_0000162259`
`DOMAIN`	`1 77`	`77`	`Lipoyl-binding.`
`ACT_SITE`	`391 391`		`Potential.`
`ACT_SITE`	`395 395`		`Potential.`
`BINDING`	`44 44`		`Lipoyl (covalent) (Potential).`

Sequence information

Length: 420 AA [This is the length of the unprocessed precursor]

Molecular weight: 48092 Da [This is the MW of the unprocessed precursor]

CRC64: E0028D647A5CE34C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKINILVPD LPESISDATV VKWHKKIGDT VHCDDNIVDI ETDKVMLEVS SPCDGILQSI 

        70         80         90        100        110        120 
LEKEGKVVIS QQTLGEINKS TVVDNHLSNN HIIEKEDNLL KKEEKYITTE EKKEIEYLLK 

       130        140        150        160        170        180 
DNHKHLTPSM RRSVKIHNIN NGFLNQVIET SKKTNFENII KEEKKESNQI LFNHNIFNAN 

       190        200        210        220        230        240 
ENNKNNNNKV TNRVKMTRLR QRIAERLLDS KNNTAMLTTF HEVNMKPIIL LRKKYGEDFE 

       250        260        270        280        290        300 
KKHNVRIGFM SFFVKAVIQA LKNFPEINAY IDQTDIVFYK NFDISIAIST PRGLITPVIR 

       310        320        330        340        350        360 
NADTMTMAEI EKKIKDFSIK GLQNKINIKE LMGGNFTITN GGVFGSLMST PIINPPQTAI 

       370        380        390        400        410        420 
LGMHVIQERP VVVNGQIKIL PMMYLALSYD HRLIDGKESV GFLINIKNIL EDFNRIAIDV

P57389 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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