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: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate.
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.

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; CAA62980.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AM260479; CAJ93421.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T44422; T44422.

RefSeq

YP_726789.1; -.

3D structure databases

ModBase

Q59106.

Family and domain databases

InterPro

IPR011603; 2oxoglutarate_DHase_E1.
IPR001017; DHase_E1.
IPR005475; Transketo_Cen_R.
Graphical view of domain structure.

PANTHER

PTHR23152; 2oxoglutarate_DH_E1; 1.

Pfam

PF00676; E1_dh; 1.
PF02779; Transket_pyr; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000157; Oxoglu_dh_E1; 1.

TIGRFAMs

TIGR00239; 2oxo_dh_E1; 1.

BLOCKS

Q59106.

Genome annotation databases

GeneID

4249723; -.

GenomeReviews

AM260479_GR; H16_A2325.

KEGG

reh:H16_A2325; -.

Phylogenomic databases

HOGENOM

Q59106; -.

Genome annotation databases

CMR

Q59106; H16_A2325.

Other

ProtoNet

Q59106.

UniRef

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

Keywords

Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 950`	`950`	`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000162160`
`CONFLICT`	`621 621`		`G -> A (in Ref. 1; CAA62980).`

Sequence information

Length: 950 AA [This is the length of the unprocessed precursor]

Molecular weight: 105996 Da [This is the MW of the unprocessed precursor]

CRC64: 531BC77561D2ECCF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMQQYQSNSY LFGGNAPYVE ELYEAYLQNP ASVPDNWRAY FDAMQNVPAV DGSNGRDIPH 

        70         80         90        100        110        120 
APIVASFAER AKQGPIRTIV ASADSDMGRK RVAATQLIAA YRNIGSHWAD LDPLKRQERP 

       130        140        150        160        170        180 
PLPDLDPAFY GFSEADLDIV FNASNTYFGK ESMSLRELLN NLRETYCGTI GFEFMYVSDQ 

       190        200        210        220        230        240 
AQKRWWQERL ETTRSKPVFT LEKKKHILDR LTAAEGLERF LHTKYVGQKR FSLEGGESFI 

       250        260        270        280        290        300 
AAMDELIQHA GSKGVQEIVI GMAHRGRLNV LVNTLGKMPA DLFAEFEGKH VDDLPAGDVK 

       310        320        330        340        350        360 
YHKGFSSDVS TEGGPVHLSL AFNPSHLEIV NPVVEGSAKA RQERRGEVGH KEVLPVQVHG 

       370        380        390        400        410        420 
DAAFAGQGVV METLNLAQTR GYGTGGSMHI VINNQIGFTT SDPRDARSTL YCTDVVKMIE 

       430        440        450        460        470        480 
APVLHVNGDD PEAVVYAMQL AVDFRMEFKK DVVVDIICFR KLGHNEQDTP AVTQPLMYKK 

       490        500        510        520        530        540 
IAQHPGTRKL YADKLAAQNL VPAEFGDEKV KAYRAAMDAG KHTADPVLSN FKNKFAVDWM 

       550        560        570        580        590        600 
PFLNRKWTDA ADTAVPVTEL KRLAERITTT PETLKLHPLV EKVVKDRANM GRGDQPLDWG 

       610        620        630        640        650        660 
MGEHLAFASL VSSGYPVRIT GQDAGRGTFT HRHAVLHDQA RERWDAGSYV PLQNVSENQA 

       670        680        690        700        710        720 
PFTVIDSVLS EEAVLGFEYG YSAAEPNALV IWEAQFGDFV NGAQVVIDQF ISSGEVKWGR 

       730        740        750        760        770        780 
ASGLTLMLPH GYEGQGPEHS SARIERFLQL CADHNMQVCQ PTTPAQIFHL LRRQMIRLFR 

       790        800        810        820        830        840 
KPLVIMTPKS LLRNKDAVSP LSDLAKGHFE TVIPDHEELN ASKVKRVIMC SGKVYYDLVN 

       850        860        870        880        890        900 
TRKEREANDT AVIRLEQLYP FPHKAVAAEL KKYPNATEIV WCQDEPQNQG AWFFVQHYIM 

       910        920        930        940        950 
ENMTDGQKLG YAGRPASASP AVGYYAKHNE QQKALLEAAF AKLKGFVLTK

Q59106 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