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Q89AJ7 (ODO1_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. 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:
Oxoglutarate dehydrogenase

EC=1.2.4.2
Gene names
Name:sucA
Ordered Locus Names:bbp_280
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length916 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 – 916916Oxoglutarate dehydrogenase
PRO_0000162189

Sequences

Sequence LengthMass (Da)Tools
Q89AJ7 [UniParc].

Last modified June 16, 2003. Version 1.
Checksum: 9421601E0BE528CB

FASTA916106,047
        10         20         30         40         50         60 
MYKNEFNSSW MSSFNSSYID NLYNKFLLDP TSIDNSWYIV FTELSKENYI NSTNKYLNNK 

        70         80         90        100        110        120 
FQDSKDTIKL TIELLINIFR TLGYKFAHLN PLDTFKNDNS LSLKKFLKSS EAFRIQDSYL 

       130        140        150        160        170        180 
VKLSQYVLDD ITTKNVYDDY KNIYCKRIGY QFMHIHNSNE MNWIKNYIET KHSNILKKKK 

       190        200        210        220        230        240 
KIQILKHLII SEMLEKYFSS KFPSIKRFSI EGAESLIPML KEVIKYTKKF NLHKIIFGMS 

       250        260        270        280        290        300 
HRGRLNVLAN ILDKPIKTIF NEFCENNSNN FNSGDVKYHM GFCCTKTIGL RKIILDLKSN 

       310        320        330        340        350        360 
PSHLEVINPV VVGSSRAYID SNDNLNDENI LPIIIHGDAA ISGQGVVQEL LNMSQARGYK 

       370        380        390        400        410        420 
VGGTIHIVVN NQIGFTTSKV KDLRTSQYCT DIAKMIDSPI FHVNADDPES VIFVTHLALN 

       430        440        450        460        470        480 
YRFCFKKDVF INLVCYRRHG HNEIDDPSIT QPVLYSKIKN HPTTATSYYN KLLLKNIINK 

       490        500        510        520        530        540 
SFLITYQKKI KKKLDVEYNL HNKKMSEKRL KCCSIVKADY INVSNTPINN ISQSDLTILA 

       550        560        570        580        590        600 
KKIFSIPNNI EVHNRVFKIY KDRLKMANNE KLFDWGASEL LAYASLLNEG ISCRLSGEDV 

       610        620        630        640        650        660 
CRGTFFHRHA VIHDQKNDSK YIPLKNIKLK QGNFYIWDSV LSEEATLAFE YGYSIDQKNT 

       670        680        690        700        710        720 
LNVWEAQFGD FANGAQIIID QFICSGEQKW NVTCNLVMLL PHGYEGQGPE HSSARIERYL 

       730        740        750        760        770        780 
QLSANNNIKI IIPTISSQIY HIIRKQAFSL IKKPLIIMSP KSLLRFPLAA SSLSELSNGK 

       790        800        810        820        830        840 
FRTVIDEIDN LDTKKVQRII LCSGKIYYDL LTQRRINQQK NIVILRIEQI YPRPTKKLSA 

       850        860        870        880        890        900 
ILYNYKDVHD YIWCQEEPCN QGAWLYHKSY LKKLLPKHSK LNYVGRSSSA SPATGYMKIH 

       910 
KEQQKKIIYD ALNISD 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO27005.1.
RefSeqNP_777900.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO27005; AAO27005; bbp_280.
GeneID1058600.
KEGGbab:bbp280.
PATRIC21245347. VBIBucAph80364_0276.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0567.
KOK00164.
OMAQHAPNKE.
OrthoDBEOG6V1M1F.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-280-MONOMER.

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_BUCBP
AccessionPrimary (citable) accession number: Q89AJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: June 11, 2014
This is version 75 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