NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1097(95)00487-4; PubMed=8867378 [NCBI, ExPASy, EBI, Israel, Japan]
Hein S., Steinbuechel A.;
"Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex.";
FEMS Microbiol. Lett. 136:231-238(1996).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1244; PubMed=16964242 [NCBI, ExPASy, EBI, Israel, Japan]
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16.";
Nat. Biotechnol. 24:1257-1262(2006).

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).
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.
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

X91877; CAA62981.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AM260479; CAJ93420.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T44423; T44423.

RefSeq

YP_726788.1; -.

3D structure databases

HSSP

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

ModBase

P52993.

Ontologies

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:0005515;	Molecular function: protein binding (inferred from electronic annotation from InterPro).
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.
IPR004167; E3_bd.
IPR006255; SucB.
Graphical view of domain structure.

Gene3D

G3DSA:4.10.320.10; E3_bd; 1.

Pfam

PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 1.
PF02817; E3_binding; 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).

Genome annotation databases

GeneID

4249724; -.

GenomeReviews

AM260479_GR; H16_A2324.

KEGG

reh:H16_A2324; -.

Phylogenomic databases

HOGENOM

P52993; -.

Genome annotation databases

CMR

P52993; H16_A2324.

Other

ProtoNet

P52993.

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`	`1 416`	`416`	`Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex.`	`PRO_0000162253`
`DOMAIN`	`1 77`	`77`	`Lipoyl-binding.`
`ACT_SITE`	`387 387`		`By similarity.`
`ACT_SITE`	`391 391`		`By similarity.`
`BINDING`	`44 44`		`Lipoyl (covalent) (Potential).`

Sequence information

Length: 416 AA [This is the length of the unprocessed precursor]

Molecular weight: 43250 Da [This is the MW of the unprocessed precursor]

CRC64: 100D839352D0A8DF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIVDVKVPQ LSESVAEATM LNWKKKPGEA VAQDEILIEI ETDKVVLEVP APSAGVLSII 

        70         80         90        100        110        120 
VKNDGDTVVA DEIIAKIDTE ATAGAAAPAA AAPAPAAAAP APAAAVAAPA AAGGVAMPSA 

       130        140        150        160        170        180 
AKLMAEAGLS AGQVAGTGKD GRITKGDALA AAAAPAAKAA PAPAAAKPAL QQVSAPVDFA 

       190        200        210        220        230        240 
ALGDRPEERV PMSRLRARIA ERLLQSQSTN AILTTFNEVN MKPVMDLRNK YKDRFEKEHG 

       250        260        270        280        290        300 
VKLGFMSFFV KAAVHALKKF PLINASIDGN DIVYHGYFDI GIAVGSPRGL VVPILRNADQ 

       310        320        330        340        350        360 
MSLADIEKKI AEFGVKARDG KLSLEELTGG TFSISNGGVF GSMLSTPIIN PPQSAILGVH 

       370        380        390        400        410 
ATKDRPVVED GQIVIRPMNY LAMSYDHRII DGREAVLGLV AMKDALEDPA RLLLDL

P52993 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