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).
SUBCELLULAR LOCATION: Mitochondrion matrix (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

CAAC02000447; CAP22897.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q623T0.

Organism-specific databases

WormBase

WBGene00024926; CBG01737.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031966;	Cellular component: mitochondrial membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0004591;	Molecular function: oxoglutarate dehydrogenase (succinyl-transferring) activity (inferred from sequence or structural similarity from UniProtKB).
GO:0030976;	Molecular function: thiamin pyrophosphate binding (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

ProtoNet

Q623T0.

Other

UniRef

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

Keywords

Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion.`
`CHAIN`	`? 1027`		`2-oxoglutarate dehydrogenase E1 component, mitochondrial.`	`PRO_0000234099`

Sequence information

Length: 1027 AA [This is the length of the unprocessed precursor]

Molecular weight: 115481 Da [This is the MW of the unprocessed precursor]

CRC64: 99584397C5540D7B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHRASLICRL ASPSRINSIR SASSYGNNTI SATPLVQQRK QSVAASVKHE PFLNGSSSVY 

        70         80         90        100        110        120 
IEQMYETWLE NPSSVHTSWD AYFRNVEAGA GPGQAFQAPP SVAYAGSMGV PSAPITSAAP 

       130        140        150        160        170        180 
ATRLDTNASV QSISDHLKIQ LLIRSYQTRG HNIADLDPLG INSADLDDTI PPELELSFYG 

       190        200        210        220        230        240 
LGERDLDREF LLPPTTFISE KKSLTLREIL QRLKEIYCTS TGVEYMHLNN LEQQDWIRRR 

       250        260        270        280        290        300 
FEAPRVTELS HDQKKVLFKR LIRSTKFEEF LAKKWPSEKR FGLEGCEVLI PAIKQVIDSS 

       310        320        330        340        350        360 
STLGVDSFVI GMPHRGRLNV LANVCRQPLA TILSQFSTLE PADEGSGDVK YHLGVCIERL 

       370        380        390        400        410        420 
NRQSQKNVKI AVVANPSHLE AVDPVVMGKV RAEAFYAGDE KCDRTMAILL HGDAAFAGQG 

       430        440        450        460        470        480 
VVLETFNLDD LPSYTTHGAI HIVVNNQIGF TTDPRSSRSS PYCTDVGRVV GCPIFHVNVD 

       490        500        510        520        530        540 
DPEAVMHVCN VAADWRKTFK KDVIVDLVCY RRHGHNELDE PMFTQPLMYQ RIKQTKTALE 

       550        560        570        580        590        600 
KYQEKILNEG VANEQYVKEE LTKYGAILED AYENAQKVTY VRNRDWLDSP WDDFFKKRDP 

       610        620        630        640        650        660 
LKLPSTGIEQ ENIEHIIGKF GSYPEGFNLH RGLERTLKGR QQMLKDNSLD WACGEALAFG 

       670        680        690        700        710        720 
SLLKEGIHVR LSGQDVERGT FSHRHHVLHD QKVDQKIYNP LNDLADPQGE YTVCNSSLSE 

       730        740        750        760        770        780 
YAVLGFELGY SMVDPNSLVI WEAQFGDFSN TAQCIIDQFV SSGQSKWIRQ SGLVMLLPHG 

       790        800        810        820        830        840 
YEGMGPEHSS ARPERFLQMC NEDDEIDLDK IAFGGTFEAQ QLHDTNWIVA NCTTPANIYH 

       850        860        870        880        890        900 
LLRRQVTMPF RKPAVVFSPK SLLRHPMARS PVEDFQSGSN FQRIIPETGA PSQNPPNVQR 

       910        920        930        940        950        960 
LVFCTGKVYY DMVAARKHVG KENDVALVRV EQLSPFPYDL VQQECRKYQG AEIIWAQEEH 

       970        980        990       1000       1010       1020 
KNMGAWSFVQ PRINSLLSID GRATKYAGRL PSSSPATGNK YTHMQEQKEM MSKVFGVPKS 


KLEGFKA

Q623T0 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