[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY. STRAIN=AJ12036; PubMed=9004499 [NCBI, ExPASy, EBI, Israel, Japan] Usuda Y., Tujimoto N., Abe C., Asakura Y., Kimura E., Kawahara Y., Kurahashi O., Matsui H.; "Molecular cloning of the Corynebacterium glutamicum ('Brevibacterium lactofermentum' AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase."; Microbiology 142:3347-3354(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."; J. Biotechnol. 104:5-25(2003).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; Nakagawa S.; "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]	INHIBITION BY ODHI. DOI=10.1074/jbc.M512515200; PubMed=16522631 [NCBI, ExPASy, EBI, Israel, Japan] Niebisch A., Kabus A., Schultz C., Weil B., Bott M.; "Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein."; J. Biol. Chem. 281:12300-12307(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) (By similarity).
CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate (By similarity).
ENZYME REGULATION: Inhibited by unphosphorylated odhI, but not by phosphorylated odhI.
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

D84102; BAA12222.2; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927151; CAF19835.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAB98522.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_600357.3; -.
YP_225421.2; -.

3D structure databases

HSSP

P07016; 1E2O. [HSSP ENTRY / PDB]

ModBase

Q8NRC3.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG1280-MON; -.

Family and domain databases

InterPro

IPR001078; 2Oxoacid_DHase.
IPR011603; 2oxoglutarate_DHase_E1.
IPR001017; DHase_E1.
IPR005475; Transketo_Cen_R.
Graphical view of domain structure.

PANTHER

PTHR23152; 2oxoglutarate_DH_E1; 1.

Pfam

PF00198; 2-oxoacid_dh; 1.
PF00676; E1_dh; 1.
PF02779; Transket_pyr; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000157; Oxoglu_dh_E1; 1.

ProDom

PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00239; 2oxo_dh_E1; 1.

BLOCKS

Q8NRC3.

Genome annotation databases

GeneID

1019114; -.
3343144; -.

GenomeReviews

BX927147_GR; cg1280.
BA000036_GR; Cgl1129.

KEGG

cgb:cg1280; -.
cgl:NCgl1084; -.

Phylogenomic databases

HOGENOM

Q8NRC3; -.

Genome annotation databases

CMR

Q8NRC3; Cgl1129.

Other

ProtoNet

Q8NRC3.

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 1257`	`1257`	`2-oxoglutarate dehydrogenase E1 component.`	`PRO_0000273521`
`CONFLICT`	`20 20`		`T -> I (in Ref. 1; BAA12222).`
`CONFLICT`	`80 80`		`T -> A (in Ref. 1; BAA12222).`
`CONFLICT`	`118 118`		`D -> A (in Ref. 1; BAA12222).`
`CONFLICT`	`274 274`		`A -> T (in Ref. 1; BAA12222).`
`CONFLICT`	`449 449`		`N -> S (in Ref. 1; BAA12222).`
`CONFLICT`	`460 460`		`N -> S (in Ref. 1; BAA12222).`
`CONFLICT`	`1003 1003`		`I -> V (in Ref. 1; BAA12222).`
`CONFLICT`	`1129 1129`		`N -> D (in Ref. 1; BAA12222).`

Sequence information

Length: 1257 AA [This is the length of the unprocessed precursor]

Molecular weight: 138757 Da [This is the MW of the unprocessed precursor]

CRC64: 96473BCB12B22ABF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLQLGLRHNQ PTTNVTVDKT KLNKPSRSKE KRRVPAVSSA STFGQNAWLV DEMFQQFQKD 

        70         80         90        100        110        120 
PKSVDKEWRE LFEAQGGPNT TPATTEAQPS APKESAKPAP KAAPAAKAAP RVETKPADKT 

       130        140        150        160        170        180 
APKAKESSVP QQPKLPEPGQ TPIRGIFKSI AKNMDISLEI PTATSVRDMP ARLMFENRAM 

       190        200        210        220        230        240 
VNDQLKRTRG GKISFTHIIG YAMVKAVMAH PDMNNSYDVI DGKPTLIVPE HINLGLAIDL 

       250        260        270        280        290        300 
PQKDGSRALV VAAIKETEKM NFSEFLAAYE DIVARSRKGK LTMDDYQGVT VSLTNPGGIG 

       310        320        330        340        350        360 
TRHSVPRLTK GQGTIIGVGS MDYPAEFQGA SEDRLAELGV GKLVTITSTY DHRVIQGAVS 

       370        380        390        400        410        420 
GEFLRTMSRL LTDDSFWDEI FDAMNVPYTP MRWAQDVPNT GVDKNTRVMQ LIEAYRSRGH 

       430        440        450        460        470        480 
LIADTNPLSW VQPGMPVPDH RDLDIETHNL TIWDLDRTFN VGGFGGKETM TLREVLSRLR 

       490        500        510        520        530        540 
AAYTLKVGSE YTHILDRDER TWLQDRLEAG MPKPTQAEQK YILQKLNAAE AFENFLQTKY 

       550        560        570        580        590        600 
VGQKRFSLEG AEALIPLMDS AIDTAAGQGL DEVVIGMPHR GRLNVLFNIV GKPLASIFNE 

       610        620        630        640        650        660 
FEGQMEQGQI GGSGDVKYHL GSEGQHLQMF GDGEIKVSLT ANPSHLEAVN PVMEGIVRAK 

       670        680        690        700        710        720 
QDYLDKGVDG KTVVPLLLHG DAAFAGLGIV PETINLAKLR GYDVGGTIHI VVNNQIGFTT 

       730        740        750        760        770        780 
TPDSSRSMHY ATDYAKAFGC PVFHVNGDDP EAVVWVGQLA TEYRRRFGKD VFIDLVCYRL 

       790        800        810        820        830        840 
RGHNEADDPS MTQPKMYELI TGRETVRAQY TEDLLGRGDL SNEDAEAVVR DFHDQMESVF 

       850        860        870        880        890        900 
NEVKEGGKKQ AEAQTGITGS QKLPHGLETN ISREELLELG QAFANTPEGF NYHPRVAPVA 

       910        920        930        940        950        960 
KKRVSSVTEG GIDWAWGELL AFGSLANSGR LVRLAGEDSR RGTFTQRHAV AIDPATAEEF 

       970        980        990       1000       1010       1020 
NPLHELAQSK GNNGKFLVYN SALTEYAGMG FEYGYSVGNE DSIVAWEAQF GDFANGAQTI 

      1030       1040       1050       1060       1070       1080 
IDEYVSSGEA KWGQTSKLIL LLPHGYEGQG PDHSSARIER FLQLCAEGSM TVAQPSTPAN 

      1090       1100       1110       1120       1130       1140 
HFHLLRRHAL SDLKRPLVIF TPKSMLRNKA AASAPEDFTE VTKFQSVIND PNVADAAKVK 

      1150       1160       1170       1180       1190       1200 
KVMLVSGKLY YELAKRKEKD GRDDIAIVRI EMLHPIPFNR ISEALAGYPN AEEVLFVQDE 

      1210       1220       1230       1240       1250 
PANQGPWPFY QEHLPELIPN MPKMRRVSRR AQSSTATGVA KVHQLEEKQL IDEAFEA

Q8NRC3 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