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Q59106

- ODO1_CUPNH

UniProt

Q59106 - ODO1_CUPNH

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Protein

2-oxoglutarate dehydrogenase E1 component

Gene
odhA, H16_A2325
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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

Cofactori

Thiamine pyrophosphate.

GO - Molecular functioni

  1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-EC
  2. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
  2. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-2293-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
Alternative name(s):
Alpha-ketoglutarate dehydrogenase
Gene namesi
Name:odhA
Ordered Locus Names:H16_A2325
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9509502-oxoglutarate dehydrogenase E1 componentPRO_0000162160Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

STRINGi381666.H16_A2325.

Structurei

3D structure databases

ProteinModelPortaliQ59106.
SMRiQ59106. Positions 88-941.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259586.
KOiK00164.
OMAiGFTTAPH.
OrthoDBiEOG6V1M1F.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59106-1 [UniParc]FASTAAdd to Basket

« Hide

MMQQYQSNSY LFGGNAPYVE ELYEAYLQNP ASVPDNWRAY FDAMQNVPAV    50
DGSNGRDIPH APIVASFAER AKQGPIRTIV ASADSDMGRK RVAATQLIAA 100
YRNIGSHWAD LDPLKRQERP PLPDLDPAFY GFSEADLDIV FNASNTYFGK 150
ESMSLRELLN NLRETYCGTI GFEFMYVSDQ AQKRWWQERL ETTRSKPVFT 200
LEKKKHILDR LTAAEGLERF LHTKYVGQKR FSLEGGESFI AAMDELIQHA 250
GSKGVQEIVI GMAHRGRLNV LVNTLGKMPA DLFAEFEGKH VDDLPAGDVK 300
YHKGFSSDVS TEGGPVHLSL AFNPSHLEIV NPVVEGSAKA RQERRGEVGH 350
KEVLPVQVHG DAAFAGQGVV METLNLAQTR GYGTGGSMHI VINNQIGFTT 400
SDPRDARSTL YCTDVVKMIE APVLHVNGDD PEAVVYAMQL AVDFRMEFKK 450
DVVVDIICFR KLGHNEQDTP AVTQPLMYKK IAQHPGTRKL YADKLAAQNL 500
VPAEFGDEKV KAYRAAMDAG KHTADPVLSN FKNKFAVDWM PFLNRKWTDA 550
ADTAVPVTEL KRLAERITTT PETLKLHPLV EKVVKDRANM GRGDQPLDWG 600
MGEHLAFASL VSSGYPVRIT GQDAGRGTFT HRHAVLHDQA RERWDAGSYV 650
PLQNVSENQA PFTVIDSVLS EEAVLGFEYG YSAAEPNALV IWEAQFGDFV 700
NGAQVVIDQF ISSGEVKWGR ASGLTLMLPH GYEGQGPEHS SARIERFLQL 750
CADHNMQVCQ PTTPAQIFHL LRRQMIRLFR KPLVIMTPKS LLRNKDAVSP 800
LSDLAKGHFE TVIPDHEELN ASKVKRVIMC SGKVYYDLVN TRKEREANDT 850
AVIRLEQLYP FPHKAVAAEL KKYPNATEIV WCQDEPQNQG AWFFVQHYIM 900
ENMTDGQKLG YAGRPASASP AVGYYAKHNE QQKALLEAAF AKLKGFVLTK 950
Length:950
Mass (Da):105,996
Last modified:January 23, 2007 - v2
Checksum:i531BC77561D2ECCF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti621 – 6211G → A in CAA62980. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91877 Genomic DNA. Translation: CAA62980.1.
AM260479 Genomic DNA. Translation: CAJ93421.1.
PIRiT44422.
RefSeqiYP_726789.1. NC_008313.1.

Genome annotation databases

EnsemblBacteriaiCAJ93421; CAJ93421; H16_A2325.
GeneIDi4249723.
KEGGireh:H16_A2325.
PATRICi35234169. VBIRalEut6770_2731.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91877 Genomic DNA. Translation: CAA62980.1 .
AM260479 Genomic DNA. Translation: CAJ93421.1 .
PIRi T44422.
RefSeqi YP_726789.1. NC_008313.1.

3D structure databases

ProteinModelPortali Q59106.
SMRi Q59106. Positions 88-941.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 381666.H16_A2325.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ93421 ; CAJ93421 ; H16_A2325 .
GeneIDi 4249723.
KEGGi reh:H16_A2325.
PATRICi 35234169. VBIRalEut6770_2731.

Phylogenomic databases

eggNOGi COG0567.
HOGENOMi HOG000259586.
KOi K00164.
OMAi GFTTAPH.
OrthoDBi EOG6V1M1F.

Enzyme and pathway databases

BioCyci CNEC381666:GJUJ-2293-MONOMER.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
InterProi IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Entry informationi

Entry nameiODO1_CUPNH
AccessioniPrimary (citable) accession number: Q59106
Secondary accession number(s): Q0K9A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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