[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1371/journal.pone.0001120; PubMed=17971880 [NCBI, ExPASy, EBI, Israel, Japan] Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.; "Molecular correlates of host specialization in Staphylococcus aureus."; PLoS ONE 2:E1120-E1120(2007).

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

AJ938182; CAI80958.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_416746.1; -.

3D structure databases

ModBase

Q2YY05.

Enzyme and pathway databases

BioCyc

SAUR273036:SAB1269C-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

Q2YY05.

Genome annotation databases

GeneID

3793631; -.

GenomeReviews

AJ938182_GR; SAB1269c.

KEGG

sab:SAB1269c; -.

NMPDR

fig|273036.3.peg.1104; -.

Phylogenomic databases

HOGENOM

Q2YY05; -.

Genome annotation databases

CMR

Q2YY05; SAB1269c.

Other

ProtoNet

Q2YY05.

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`	`1 932`	`932`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_1000065704`

Sequence information

Length: 932 AA [This is the length of the unprocessed precursor]

Molecular weight: 105364 Da [This is the MW of the unprocessed precursor]

CRC64: A8642ACB91D4A5B0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND DSIVPSLKST 

        70         80         90        100        110        120 
SSQNSDGTIK RVMRLIDNIR QYGHLKADIY PVNPPKRKHV PKLEIEDFDL DQQTLEGISA 

       130        140        150        160        170        180 
GIVSDHFADI YDNAYEAILR MEKRYKGPIA FEYTHINNNT ERGWLKRRIE TPYKVTLNNN 

       190        200        210        220        230        240 
EKRALFKQLA YVEGFEKYLH KNFVGAKRFS IEGVDALVPM LQRTITIAAK EGIKNIQIGM 

       250        260        270        280        290        300 
AHRGRLNVLT HVLEKPYEMM ISEFMHTDPM KFLPEDGSLQ LTAGWTGDVK YHLGGIKTTD 

       310        320        330        340        350        360 
SYGTMQRIAL ANNPSHLEIV APVVEGRTRA AQDDTQRAGA PTTDHHKAMP IIIHGDGAYP 

       370        380        390        400        410        420 
GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA RSTTYSTDVA KGYDVPIFHV 

       430        440        450        460        470        480 
NADDVEATIE AIDIAMEFRK EFHKDVVIDL VGYRRFGHNE MDEPSITNPV PYQNIRKNDS 

       490        500        510        520        530        540 
VEYVFGKKLV NEGVISEDEM HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPAELALPLQ 

       550        560        570        580        590        600 
ADEQSFTFDH LKEINDALLT YPDGFNILKK LNKVLKKRHE PFNKEDGLVD WAQAEQLAFA 

       610        620        630        640        650        660 
TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPNQKATF DIHNSPLSEA 

       670        680        690        700        710        720 
AVVGFEYGYN VENKKSFNIW EAQYGDFANM SQMIFDNFLF SSRSKWGERS GLTLFLPHAY 

       730        740        750        760        770        780 
EGQGPEHSSA RLERFLQLAA ENNCTVVNLS SSSNYFHLLR AQAASLDSEQ MRPLVVMSPK 

       790        800        810        820        830        840 
SLLRNKTVAK PIDEFTSGGF EPILTESYQA DKVTKVILAT GKMFIDLKEA LAKNPDESVL 

       850        860        870        880        890        900 
LVAIERLYPF PEEEIETLLA QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY 

       910        920        930 
HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN

Q2YY05 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