2-oxoglutarate dehydrogenase E1 component - Corynebacterium glutamicum

Preferred order of sections

Names and origin

Protein names

Recommended name:
2-oxoglutarate dehydrogenase E1 component
EC=1.2.4.2

Alternative name(s):
Alpha-ketoglutarate dehydrogenase

Gene names

Name:	odhA
Ordered Locus Names:	Cgl1129, cg1280

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	1257 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO₂. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. UniProtKB P0AFG3
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO₂. Ref.1
Cofactor	Thiamine pyrophosphate By similarity. UniProtKB P0AFG3
Enzyme regulation	Inhibited by unphosphorylated odhI, but not by phosphorylated odhI. Ref.4
Subunit structure	Homodimer By similarity. UniProtKB P0AFG3
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.
Sequence caution	The sequence BAA12222.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: EC thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring acyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1257

1257

2-oxoglutarate dehydrogenase E1 component

PRO_0000273521

Experimental info

Sequence conflict

20

1

T → I in BAA12222. Ref.1

Sequence conflict

80

1

T → A in BAA12222. Ref.1

Sequence conflict

118

1

D → A in BAA12222. Ref.1

Sequence conflict

274

1

A → T in BAA12222. Ref.1

Sequence conflict

449

1

N → S in BAA12222. Ref.1

Sequence conflict

460

1

N → S in BAA12222. Ref.1

Sequence conflict

1003

1

I → V in BAA12222. Ref.1

Sequence conflict

1129

1

N → D in BAA12222. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q8NRC3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 96473BCB12B22ABF
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FASTA

1,257

138,757

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the Corynebacterium glutamicum ('Brevibacterium lactofermentum' AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase." Usuda Y., Tujimoto N., Abe C., Asakura Y., Kimura E., Kawahara Y., Kurahashi O., Matsui H. Microbiology 142:3347-3354(1996) [PubMed: 9004499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY. Strain: AJ12036.
[2]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." 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. Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein." Niebisch A., Kabus A., Schultz C., Weil B., Bott M. J. Biol. Chem. 281:12300-12307(2006) [PubMed: 16522631] [Abstract] Cited for: INHIBITION BY ODHI.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D84102 Genomic DNA. Translation: BAA12222.2. Different initiation. BX927151 Genomic DNA. Translation: CAF19835.1. BA000036 Genomic DNA. Translation: BAB98522.1.
RefSeq	NP_600357.3. NC_003450.3. YP_225421.2. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NRC3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1019114. 3343144.
GenomeReviews	Gene locus Cgl1129 in contig BA000036_GR. Gene locus cg1280 in contig BX927147_GR.
KEGG	cgb:cg1280. cgl:NCgl1084.
PATRIC	21494302. VBICorGlu203724_1108.
Phylogenomic databases
HOGENOM	HBG289950.
OMA	EGDEPAF.
PhylomeDB	Q8NRC3.
ProtClustDB	PRK12270.
Enzyme and pathway databases
BioCyc	CGLU196627:CG1280-MONOMER.
Family and domain databases
InterPro	IPR001078. 2-oxoacid_DH_actylTfrase. IPR011603. 2oxoglutarate_DH_E1. IPR023213. CAT-like_dom. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
Gene3D	G3DSA:3.30.559.10. CAT-like_dom. 1 hit.
KO	K00164.
PANTHER	PTHR23152. 2oxoglutarate_DH_E1. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODO1_CORGL

Accession

Primary (citable) accession number: Q8NRC3
Secondary accession number(s): P96746, Q6M641

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents