IDENTIFICATION BY MASS SPECTROMETRY.
Vaezzadeh A.R., Deshusses J., Lescuye P., Hochstrasser D.F.;
"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315.";
Submitted (OCT-2007) to UniProtKB.

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

BA000018; BAB42505.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E89918; E89918.

RefSeq

NP_374526.1; -.

3D structure databases

ModBase

Q99U74.

Enzyme and pathway databases

BioCyc

SAUR158879:SA1245-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).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

GeneID

1124084; -.

GenomeReviews

BA000018_GR; SA1245.

KEGG

sau:SA1245; -.

Phylogenomic databases

HOGENOM

Q99U74; -.

Genome annotation databases

CMR

Q99U74; SA1245.

Other

ProtoNet

Q99U74.

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`	`1 910`	`910`		`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000162178`

Sequence information

Length: 910 AA [This is the length of the unprocessed precursor]

Molecular weight: 103112 Da [This is the MW of the unprocessed precursor]

CRC64: 7803AAED537CF247 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKRV MRLIDNIRQY 

        70         80         90        100        110        120 
GHLKADIYPV NPPKRKHVPK LEIEDFDLDQ QTLEGISAGI VSDHFADIYD NAYEAILRME 

       130        140        150        160        170        180 
KRYKGPIAFE YTHINNNTER GWLKRRIETP YKVTLNNNEK RALFKQLAYV EGFEKYLHKN 

       190        200        210        220        230        240 
FVGAKRFSIE GVDALVPMLQ RTITIAAKEG IKNIQIGMAH RGRLNVLTHV LEKPYEMMIS 

       250        260        270        280        290        300 
EFMHTDPMKF LPEDGSLQLT AGWTGDVKYH LGGIKTTDSY GTMQRIALAN NPSHLEIVAP 

       310        320        330        340        350        360 
VVEGRTRAAQ DDTQRAGAPT TDHHKAMPII IHGDAAYPGQ GINFETMNLG NLKGYSTGGS 

       370        380        390        400        410        420 
LHIITNNRIG FTTEPIDARS TTYSTDVAKG YDVPIFHVNA DDVEATIEAI DIAMEFRKEF 

       430        440        450        460        470        480 
HKDVVIDLVG YRRFGHNEMD EPSITNPVPY QNIRKHDSVE YVFGKKLVNE GVISEDEMHS 

       490        500        510        520        530        540 
FIEQVQKELR QAHDKINKAD KMDNPDMEKP AELALPLQAD EQSFTFDHLK EINDALLTYP 

       550        560        570        580        590        600 
DGFNILKKLN KVLEKRHEPF NKEDGLVDWA QAEQLAFATI LQDGTPIRLT GQDSERGTFS 

       610        620        630        640        650        660 
HRHAVLHDEQ TGETYTPLHH VPDQKATFDI HNSPLSEAAV VGFEYGYNVE NKKSFNIWEA 

       670        680        690        700        710        720 
QYGDFANMSQ MIFDNFLFSS RSKWGERSGL TLFLPHAYEG QGPEHSSARL ERFLQLAAEN 

       730        740        750        760        770        780 
NCTVVNLSSS SNYFHLLRAQ AASLDSEQMR PLVVMSPKSL LRNKTVAKPI DEFTSGGFEP 

       790        800        810        820        830        840 
ILTESYQADK VTKVILATGK MFIDLKEALA KNPDESVLLV AIERLYPFPE EEIEALLAQL 

       850        860        870        880        890        900 
PKLEEVSWVQ EEPKNQGAWL YVYPYVKVLV ADKYDLSYHG RIQRAAPAEG DGEIHKLVQN 

       910 
KIIENALKNN

Q99U74 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