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Q8NRC3 (ODO12_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-oxoglutarate dehydrogenase E1/E2 component

Short name=ODH E1/E2 component

Including the following 2 domains:

  1. 2-oxoglutarate dehydrogenase E1 component
    Short name=ODH E1 component
    EC=1.2.4.2
    Alternative name(s):
    Alpha-ketoglutarate dehydrogenase E1 component
    Short name=KDH E1 component
  2. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
    EC=2.3.1.61
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex E2 component
    Short name=ODH E2 component
    Short name=OGDC-E2
    Dihydrolipoamide succinyltransferase
Gene names
Name:odhA
Ordered Locus Names:Cgl1129, cg1280
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length1221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the E1 and E2 reactions as part of 2-oxoglutarate dehydrogenase (ODH) activity, to convert 2-oxoglutarate to succinyl-CoA and CO2. OdhA has reductase activity with 2-oxoglutarate but does not react with pyruvate, and also displays transsuccinylase but no transacetylase activity. Since OdhA is not lipoylated, the succinyltransferase activity of its E2 domain is dependent on lipoyl residues of the acetyltransferase AceF. Ref.4

Catalytic activity

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. Ref.1 Ref.4

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine. Ref.1 Ref.4

Cofactor

Magnesium By similarity.

Thiamine pyrophosphate By similarity. UniProtKB P0AFG3

Enzyme regulation

Inhibited by unphosphorylated OdhI, but not by phosphorylated OdhI. Ref.5 Ref.7

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.

Subunit structure

Homodimer By similarity. Part of an unusual ODH/PDH supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together with OdhA (E1+E2). Interacts with the FHA domain of unphosphorylated OdhI via its C-terminal dehydrogenase domain. Ref.5 Ref.7 UniProtKB P0AFG3

Domain

OdhA is a fusion protein with two major domains exhibiting structural features of an E1 and E2 protein, and a short sequence stretch of E1 localized at the N-terminus, which is connected by a linker region to the rest of the protein. Deletion of individual parts of odhA show that all parts of odhA are required for a functional tricarboxylic acid cycle in C.glutamicum; the ODH activity is in fact completely abolished in each of these mutants, and the PDH activity is significantly reduced, which could indicate that the overall structure of the supercomplex is disturbed. Ref.4 Ref.7

Disruption phenotype

Strains lacking this gene completely lack 2-oxoglutarate dehydrogenase activity. Deletion of odhA also causes L-glutamate overproduction and accumulation during growth. Ref.6

Miscellaneous

Is non-lipoylated. In contrast, the E2 component AceF is the prominent lipoylated protein in C.glutamicum.

Sequence similarities

In the N-terminal section; belongs to the alpha-ketoglutarate dehydrogenase family.

In the C-terminal section; belongs to the 2-oxoacid dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.014 mM for 2-oxoglutarate Ref.4

Sequence caution

The sequence BAB98522.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAF19835.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

odhIQ8NQJ32EBI-7868591,EBI-7868645

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 122112202-oxoglutarate dehydrogenase E1/E2 component
PRO_0000273521

Regions

Region2 – 40392-oxoglutarate dehydrogenase E1, N-terminal part
Region41 – 8949Linker
Region90 – 337248Succinyltransferase E2
Region338 – 12218842-oxoglutarate dehydrogenase E1, C-terminal part
Region543 – 5442Thiamine pyrophosphate binding By similarity
Region608 – 6103Thiamine pyrophosphate binding By similarity
Region645 – 6473Thiamine pyrophosphate binding By similarity

Sites

Active site3161Proton acceptor; for succinyltransferase activity Ref.4
Metal binding6451Magnesium By similarity
Metal binding6781Magnesium By similarity
Metal binding6801Magnesium; via carbonyl oxygen By similarity
Binding site58312-oxoglutarate By similarity
Binding site60812-oxoglutarate By similarity
Binding site9491Thiamine pyrophosphate By similarity
Binding site101712-oxoglutarate By similarity

Experimental info

Mutagenesis2581T → A: Loss of E2 succinyltransferase activity, but nearly no effect on E1 dehydrogenase activity. Ref.4
Mutagenesis3161H → C: Loss of E2 succinyltransferase activity, and 2-fold reduction in E1 dehydrogenase activity. Ref.4
Mutagenesis3201Q → D: Slight reduction in E2 succinyltransferase activity and in E1 dehydrogenase activity. Ref.4
Sequence conflict441T → A in BAA12222. Ref.1
Sequence conflict821D → A in BAA12222. Ref.1
Sequence conflict2381A → T in BAA12222. Ref.1
Sequence conflict4131N → S in BAA12222. Ref.1
Sequence conflict4241N → S in BAA12222. Ref.1
Sequence conflict9671I → V in BAA12222. Ref.1
Sequence conflict10931N → D in BAA12222. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8NRC3 [UniParc].

Last modified November 28, 2012. Version 2.
Checksum: BF0A1827EA1B0080

FASTA1,221134,664
        10         20         30         40         50         60 
MSSASTFGQN AWLVDEMFQQ FQKDPKSVDK EWRELFEAQG GPNTTPATTE AQPSAPKESA 

        70         80         90        100        110        120 
KPAPKAAPAA KAAPRVETKP ADKTAPKAKE SSVPQQPKLP EPGQTPIRGI FKSIAKNMDI 

       130        140        150        160        170        180 
SLEIPTATSV RDMPARLMFE NRAMVNDQLK RTRGGKISFT HIIGYAMVKA VMAHPDMNNS 

       190        200        210        220        230        240 
YDVIDGKPTL IVPEHINLGL AIDLPQKDGS RALVVAAIKE TEKMNFSEFL AAYEDIVARS 

       250        260        270        280        290        300 
RKGKLTMDDY QGVTVSLTNP GGIGTRHSVP RLTKGQGTII GVGSMDYPAE FQGASEDRLA 

       310        320        330        340        350        360 
ELGVGKLVTI TSTYDHRVIQ GAVSGEFLRT MSRLLTDDSF WDEIFDAMNV PYTPMRWAQD 

       370        380        390        400        410        420 
VPNTGVDKNT RVMQLIEAYR SRGHLIADTN PLSWVQPGMP VPDHRDLDIE THNLTIWDLD 

       430        440        450        460        470        480 
RTFNVGGFGG KETMTLREVL SRLRAAYTLK VGSEYTHILD RDERTWLQDR LEAGMPKPTQ 

       490        500        510        520        530        540 
AEQKYILQKL NAAEAFENFL QTKYVGQKRF SLEGAEALIP LMDSAIDTAA GQGLDEVVIG 

       550        560        570        580        590        600 
MPHRGRLNVL FNIVGKPLAS IFNEFEGQME QGQIGGSGDV KYHLGSEGQH LQMFGDGEIK 

       610        620        630        640        650        660 
VSLTANPSHL EAVNPVMEGI VRAKQDYLDK GVDGKTVVPL LLHGDAAFAG LGIVPETINL 

       670        680        690        700        710        720 
AKLRGYDVGG TIHIVVNNQI GFTTTPDSSR SMHYATDYAK AFGCPVFHVN GDDPEAVVWV 

       730        740        750        760        770        780 
GQLATEYRRR FGKDVFIDLV CYRLRGHNEA DDPSMTQPKM YELITGRETV RAQYTEDLLG 

       790        800        810        820        830        840 
RGDLSNEDAE AVVRDFHDQM ESVFNEVKEG GKKQAEAQTG ITGSQKLPHG LETNISREEL 

       850        860        870        880        890        900 
LELGQAFANT PEGFNYHPRV APVAKKRVSS VTEGGIDWAW GELLAFGSLA NSGRLVRLAG 

       910        920        930        940        950        960 
EDSRRGTFTQ RHAVAIDPAT AEEFNPLHEL AQSKGNNGKF LVYNSALTEY AGMGFEYGYS 

       970        980        990       1000       1010       1020 
VGNEDSIVAW EAQFGDFANG AQTIIDEYVS SGEAKWGQTS KLILLLPHGY EGQGPDHSSA 

      1030       1040       1050       1060       1070       1080 
RIERFLQLCA EGSMTVAQPS TPANHFHLLR RHALSDLKRP LVIFTPKSML RNKAAASAPE 

      1090       1100       1110       1120       1130       1140 
DFTEVTKFQS VINDPNVADA AKVKKVMLVS GKLYYELAKR KEKDGRDDIA IVRIEMLHPI 

      1150       1160       1170       1180       1190       1200 
PFNRISEALA GYPNAEEVLF VQDEPANQGP WPFYQEHLPE LIPNMPKMRR VSRRAQSSTA 

      1210       1220 
TGVAKVHQLE EKQLIDEAFE A 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY.
Strain: AJ12036.
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"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. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"The E2 domain of OdhA of Corynebacterium glutamicum has succinyltransferase activity dependent on lipoyl residues of the acetyltransferase AceF."
Hoffelder M., Raasch K., van Ooyen J., Eggeling L.
J. Bacteriol. 192:5203-5211(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8, FUNCTION AS E1 AND E2 COMPONENT OF ODH, CATALYTIC ACTIVITY, KINETIC PARAMETERS, DOMAIN, LACK OF LIPOYLATION, ACTIVE SITE, MUTAGENESIS OF THR-258; HIS-316 AND GLN-320.
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[5]"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] [Europe PMC] [Abstract]
Cited for: INHIBITION BY ODHI, IDENTIFICATION IN THE ODH/PDH COMPLEX.
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[6]"Altered metabolic flux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum."
Asakura Y., Kimura E., Usuda Y., Kawahara Y., Matsui K., Osumi T., Nakamatsu T.
Appl. Environ. Microbiol. 73:1308-1319(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.
[7]"The FHA domain of OdhI interacts with the carboxyterminal 2-oxoglutarate dehydrogenase domain of OdhA in Corynebacterium glutamicum."
Krawczyk S., Raasch K., Schultz C., Hoffelder M., Eggeling L., Bott M.
FEBS Lett. 584:1463-1468(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, ENZYME REGULATION, INTERACTION WITH ODHI.
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D84102 Genomic DNA. Translation: BAA12222.2.
BA000036 Genomic DNA. Translation: BAB98522.1. Different initiation.
BX927151 Genomic DNA. Translation: CAF19835.1. Different initiation.
RefSeqNP_600357.3. NC_003450.3.
YP_225421.2. NC_006958.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8NRC3. 1 interaction.
MINTMINT-7713226.
STRING196627.cg1280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98522; BAB98522; BAB98522.
CAF19835; CAF19835; cg1280.
GeneID1019114.
3343144.
KEGGcgb:cg1280.
cgl:NCgl1084.
PATRIC21494302. VBICorGlu203724_1108.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000259587.
KOK00164.
OrthoDBEOG6V1M1F.
ProtClustDBPRK12270.

Enzyme and pathway databases

BioCycCGLU196627:GJDM-1116-MONOMER.
UniPathwayUPA00223; UER00997.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR011603. 2oxoglutarate_DH_E1.
IPR023213. CAT-like_dom.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODO12_CORGL
AccessionPrimary (citable) accession number: Q8NRC3
Secondary accession number(s): P96746, Q6M641
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: November 28, 2012
Last modified: December 11, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways