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Q59106 (ODO1_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-oxoglutarate dehydrogenase E1 component

EC=1.2.4.2
Alternative name(s):
Alpha-ketoglutarate dehydrogenase
Gene names
Name:odhA
Ordered Locus Names:H16_A2325
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length950 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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).

Catalytic activity

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

Cofactor

Thiamine pyrophosphate.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandThiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

thiamine pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9509502-oxoglutarate dehydrogenase E1 component
PRO_0000162160

Experimental info

Sequence conflict6211G → A in CAA62980. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59106 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 531BC77561D2ECCF

FASTA950105,996
        10         20         30         40         50         60 
MMQQYQSNSY LFGGNAPYVE ELYEAYLQNP ASVPDNWRAY FDAMQNVPAV DGSNGRDIPH 

        70         80         90        100        110        120 
APIVASFAER AKQGPIRTIV ASADSDMGRK RVAATQLIAA YRNIGSHWAD LDPLKRQERP 

       130        140        150        160        170        180 
PLPDLDPAFY GFSEADLDIV FNASNTYFGK ESMSLRELLN NLRETYCGTI GFEFMYVSDQ 

       190        200        210        220        230        240 
AQKRWWQERL ETTRSKPVFT LEKKKHILDR LTAAEGLERF LHTKYVGQKR FSLEGGESFI 

       250        260        270        280        290        300 
AAMDELIQHA GSKGVQEIVI GMAHRGRLNV LVNTLGKMPA DLFAEFEGKH VDDLPAGDVK 

       310        320        330        340        350        360 
YHKGFSSDVS TEGGPVHLSL AFNPSHLEIV NPVVEGSAKA RQERRGEVGH KEVLPVQVHG 

       370        380        390        400        410        420 
DAAFAGQGVV METLNLAQTR GYGTGGSMHI VINNQIGFTT SDPRDARSTL YCTDVVKMIE 

       430        440        450        460        470        480 
APVLHVNGDD PEAVVYAMQL AVDFRMEFKK DVVVDIICFR KLGHNEQDTP AVTQPLMYKK 

       490        500        510        520        530        540 
IAQHPGTRKL YADKLAAQNL VPAEFGDEKV KAYRAAMDAG KHTADPVLSN FKNKFAVDWM 

       550        560        570        580        590        600 
PFLNRKWTDA ADTAVPVTEL KRLAERITTT PETLKLHPLV EKVVKDRANM GRGDQPLDWG 

       610        620        630        640        650        660 
MGEHLAFASL VSSGYPVRIT GQDAGRGTFT HRHAVLHDQA RERWDAGSYV PLQNVSENQA 

       670        680        690        700        710        720 
PFTVIDSVLS EEAVLGFEYG YSAAEPNALV IWEAQFGDFV NGAQVVIDQF ISSGEVKWGR 

       730        740        750        760        770        780 
ASGLTLMLPH GYEGQGPEHS SARIERFLQL CADHNMQVCQ PTTPAQIFHL LRRQMIRLFR 

       790        800        810        820        830        840 
KPLVIMTPKS LLRNKDAVSP LSDLAKGHFE TVIPDHEELN ASKVKRVIMC SGKVYYDLVN 

       850        860        870        880        890        900 
TRKEREANDT AVIRLEQLYP FPHKAVAAEL KKYPNATEIV WCQDEPQNQG AWFFVQHYIM 

       910        920        930        940        950 
ENMTDGQKLG YAGRPASASP AVGYYAKHNE QQKALLEAAF AKLKGFVLTK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex."
Hein S., Steinbuechel A.
FEMS Microbiol. Lett. 136:231-238(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91877 Genomic DNA. Translation: CAA62980.1.
AM260479 Genomic DNA. Translation: CAJ93421.1.
PIRT44422.
RefSeqYP_726789.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ59106.
SMRQ59106. Positions 88-941.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_A2325.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ93421; CAJ93421; H16_A2325.
GeneID4249723.
KEGGreh:H16_A2325.
PATRIC35234169. VBIRalEut6770_2731.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0567.
HOGENOMHOG000259586.
KOK00164.
OMAHILRRQL.
OrthoDBEOG6V1M1F.
ProtClustDBPRK09404.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-2293-MONOMER.

Family and domain databases

InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00676. 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 nameODO1_CUPNH
AccessionPrimary (citable) accession number: Q59106
Secondary accession number(s): Q0K9A0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 91 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