NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.187.21.7292-7308.2005; PubMed=16237012 [NCBI, ExPASy, EBI, Israel, Japan]
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.;
"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species.";
J. Bacteriol. 187:7292-7308(2005).

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: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate (By similarity).
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

AP006716; BAE04801.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_253407.1; -.

3D structure databases

ModBase

Q4L6C4.

Enzyme and pathway databases

BioCyc

SHAE279808:SH1492-MON; -.

Ontologies

GO:0004591;	Molecular function: oxoglutarate dehydrogenase (succinyl-transferring) activity (inferred from electronic annotation from HAMAP).
GO:0030976;	Molecular function: thiamin pyrophosphate binding (inferred from electronic annotation from HAMAP).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01169; -; 1.
PBIL [Tree]

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

Q4L6C4.

Genome annotation databases

3481998; -.

AP006716_GR; SH1492.

sha:SH1492; -.

fig|279808.3.peg.2139; -.

Phylogenomic databases

HOGENOM

Q4L6C4; -.

Genome annotation databases

CMR

Q4L6C4; SH1492.

Other

ProtoNet

Q4L6C4.

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`	`1 934`	`934`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000162184`

Sequence information

Length: 934 AA [This is the length of the unprocessed precursor]

Molecular weight: 105479 Da [This is the MW of the unprocessed precursor]

CRC64: 7D9E801A49E880E9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKDNKDVTE APVNFGANLG LMLDLYDDYL QDPSSVPDDL QVLFSTIKNG EAHVAAKSTT 

        70         80         90        100        110        120 
EGSGSSAGDG TIKRIMRLID NIRQYGHLKA DIYPVNAPKR TNLPKLEIEE FNLDKETLEN 

       130        140        150        160        170        180 
VSAEIVSDHF KDIYDNAYEA IERMEKRYKG PIAFEYNHIN NNKERTWLKR RIETPYRANI 

       190        200        210        220        230        240 
NNDERKKLFD TLAHVEGFEK YLHKNFVGAK RFSIEGVDTL VPMLQHTLKR AAEIEINNIQ 

       250        260        270        280        290        300 
IGMAHRGRLN VLTHVLEKPY EMMISEFMHT DPMKFLPEDG SLELTAGWTG DVKYHLGGVK 

       310        320        330        340        350        360 
TTSSYGIEQR ISLANNPSHL EIVAPVVIGK TRASQDDTKH AGKPTTDFHK GMPIIIHGDA 

       370        380        390        400        410        420 
AYPGQGINFE TMNLSNLDGY STGGALHIIT NNRIGFTTEP VDGRSTTYST DIAKGYDVPI 

       430        440        450        460        470        480 
LHVNADDVEA TIEAIDIAME FRKEFHKDFV IDLVGYRRYG HNEMDEPSIT NPLPYHNIRK 

       490        500        510        520        530        540 
HDSVEIIYGN KLVEDGVISK EQMEDVMDKV QKEMRAAQDK IDKSDKMDNP DMERPESLQE 

       550        560        570        580        590        600 
PLQSDDKDFS VDHLKEINDA MLTYPEDFHV LKKLNKVLEK RREPFESENG LVDWAQAEQL 

       610        620        630        640        650        660 
AFATIVQDGI SVRLTGQDSE RGTFSHRHAV LHDEENGDTF TPLHHVPNQK ATFEVHNSPL 

       670        680        690        700        710        720 
SEAAVVGFEY GYNVENKNSM NIWEAQYGDF SNMAQMMFDN FMSSARAKWG ERSGLTLFLP 

       730        740        750        760        770        780 
HAFEGQGPEH SSARLERFLQ LAAENNSTVV NLSSSSNYFH LLRAQAKSLG TEAMRPLIVM 

       790        800        810        820        830        840 
SPKSLLRNKT VAKPIDQFTS GGFKPIIVED GNKEKVTKLV LASGKMFIDL KEHLAKNPDD 

       850        860        870        880        890        900 
SILLVAVDRL YPFPEGEIKE VLNELPNLET VSWVQEEPKN QGAWLFVYPY LKSLVGNQFN 

       910        920        930 
LSYHGRIQRA APAEGDGEIH KLVQNQIIES SIEK

Q4L6C4 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