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Q92J42 (ODO1_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. 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·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:sucA
Ordered Locus Names:RC0227
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length928 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) By similarity.

Catalytic activity

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

Cofactor

Thiamine pyrophosphate By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9289282-oxoglutarate dehydrogenase E1 component
PRO_0000162195

Sequences

Sequence LengthMass (Da)Tools
Q92J42 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 4468B7CE1901591D

FASTA928103,801
        10         20         30         40         50         60 
MGEDFKKTGY LFGGNAVFVE ELYKQYLANP ASVDQTWQEF FAGIKDNNTL LNKSTAKIII 

        70         80         90        100        110        120 
PDEIKKESLN NNLSSEDLNS LKAKEMINAY RKHAHYLANL DPLGLELRKT KNDLKLNIET 

       130        140        150        160        170        180 
FGLDSGQLEE NINITDEFVG TWNCKLSELV TKFDKVYTGS IGVEFEQIEN VAGKNWLYNK 

       190        200        210        220        230        240 
LESEVTFSSE DKKTILNDLV EVEGFEQYLH TKFPGAKRFS IEGGDASIVA MSKAIDLSMH 

       250        260        270        280        290        300 
QGVSEIVIGM AHRGRLNTLT KVVGKPYKAV IADFISGSVF PDELNVSGDV KYHLGYSSDR 

       310        320        330        340        350        360 
TLEDKKIHLS LADNPSHLEA VNPIVAGKVR AKQDILGDTK RSKVKAILVH GDAAFCGQGV 

       370        380        390        400        410        420 
VAESLSMSPL AAYDIGGILH FVINNQLGFT ANAADTRASR YSTEFAKIIA APILHVNGDD 

       430        440        450        460        470        480 
IEAVLKATNI AVEYRQKFGK DVVVEIICYR KYGHNEGDEP MYTQGKMYNI IKNKLTPGNI 

       490        500        510        520        530        540 
YANELVKSGV IDNNYFAKLK EEFKAKLDKE YEQAKSYKQE AHFLGGLWQG ISRTRTQATI 

       550        560        570        580        590        600 
TGISKKTLHD LGTKLCEIPK DFAVNPKLVK LFEARKATLT ADQPIDWATA EQLAFASLLA 

       610        620        630        640        650        660 
SGTNIRLTGQ DSGRGTFSHR HSVLHNQIDG TTYIPLNNLS KEQAKYEVAD SNLSEYAVLG 

       670        680        690        700        710        720 
FEYGYSLANP KNLVLWEAQF GDFANGAQII FDQFISSSET KWLRMSGLVV LLPHAFEGQG 

       730        740        750        760        770        780 
PEHSSARLER FLQLAAENNM YVTYPTTPAS IFHLLRRQIL DDTRKPLIVM SPKSLLRHKY 

       790        800        810        820        830        840 
AVSKLDELGE NTTFLPVLDE VTKVDTNNIT KVILCSGKVY YDLFEMRGNN SNIAIIRLEQ 

       850        860        870        880        890        900 
LYPFEKKLVA SLLKKYNRTQ EFIWCQEEPK NMGTWCYIVS HLNDALKEAG IKNEFKYVGR 

       910        920 
EESASPAVGS LQVHNKQQEK LLRTALGI 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL02765.1.
PIRC97728.
RefSeqNP_359864.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92J42.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0227.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02765; AAL02765; RC0227.
GeneID927961.
KEGGrco:RC0227.
PATRIC17887605. VBIRicCon45613_0262.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0567.
HOGENOMHOG000259588.
KOK00164.
OMAGHQNANL.
OrthoDBEOG6V1M1F.

Family and domain databases

Gene3D3.40.50.970. 2 hits.
InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
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]
SUPFAMSSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODO1_RICCN
AccessionPrimary (citable) accession number: Q92J42
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 74 of the entry and version 1 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

Rickettsia conorii

(strain Malish 7): entries and gene names