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Reviewed, UniProtKB/Swiss-Prot Q8K9N3 (ODO1_BUCAP)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BUsg_292
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length923 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 – 9239232-oxoglutarate dehydrogenase E1 component
PRO_0000162188

Sequences

Sequence LengthMass (Da)Tools
Q8K9N3-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 255A7653EED01A48

FASTA923107,422
        10         20         30         40         50         60 
MKKNTLEKWF NSSWLSGNNQ NYIEKIYESY LINPKSVDIT WQDKFSDLSK KRKNILKEEK 

        70         80         90        100        110        120 
FVYKNNSFKE IKIDKQEILE KKINYIINTF RKKGYKKSLI DPLKLNEQKK YKYLEPTFYH 

       130        140        150        160        170        180 
FSEDELKKTV KIDFKNSSQY EIKIRDLYEQ LNNKYCGSIG FEYMYIENSF EKKWITKHIE 

       190        200        210        220        230        240 
LFFKENLFIK KEKIRFLKEI LYGETFEKYL GKKFSGTKRF SLEGGETLIS ILHEIIRYSK 

       250        260        270        280        290        300 
KNDVSEIILG MAHRGRLNVL VNVLNKNPQV LFNEFSGINI PKEYSGDVKY HMGGITKIKN 

       310        320        330        340        350        360 
DKKKIYLKLA YNPSHLEIVN PVVLGIARAS INQLKISENK FLSINIHGDA SIIGQGVIQE 

       370        380        390        400        410        420 
TLNMSQTEAY KIGGTIHIVI NNQIGFTTSN PKNLRSSKYC TDVAKMIQAP VFHVNADDIE 

       430        440        450        460        470        480 
ASIFAIQLAL KFKKKFKKDV FIDLVCYRRH GHNEVDDPFV TQPIMYKKIH NHPTIGQIYS 

       490        500        510        520        530        540 
NLLISEKLIT SNDIEKIIEK YTTKLVQGKN VLSQERNITF QNGNKNFFIK KQKENTQLNF 

       550        560        570        580        590        600 
LNIKDLLYSI NTIPNSIEVH NRVKKIYQER IGMADGQILL DWGTAELLAY ATILKEGISC 

       610        620        630        640        650        660 
RLSGEDISRG TFFHRHAFIH DQNNGSIYVP LQNIEKNQGK FEIWDSVLSE EAVLAFEYGY 

       670        680        690        700        710        720 
SLFPSNNLTI WEAQFGDFAN GAQVVIDQFI SSSEQKWNQK SNLVLFLPHG YEGQGPEHSS 

       730        740        750        760        770        780 
ARLERFLQLC AENNIQVCIP TVSSQIFHLL RRQIFSNVYK PLIVLTPKSL LRNNVARSSL 

       790        800        810        820        830        840 
EVLVNENFKN VINEIDKNQK EVKRIIFCSG KIYYDLLEYR NKCDINNVLL IRIEQLYPFP 

       850        860        870        880        890        900 
KDEILTILKS YSYVQDFIWC QEEPHNQGAW FYIKDLLSTL LPLNSHLNYV SRPSAASPAA 

       910        920 
GHILIHRKEQ EKLINNAFNF KIA 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE013218 Genomic DNA. Translation: AAM67847.1.
RefSeqNP_660636.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1005496.
GenomeReviewsGene locus BUsg_292 in contig AE013218_GR.
KEGGbas:BUsg292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8K9N3.
OMAQ8K9N3. QLAPFPW.

Enzyme and pathway databases

BioCycBAPH198804:BUSG292-MON.

Family and domain databases

InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR005475. Transketolase_central-reg.
[Graphical view]
PANTHERPTHR23152. 2oxoglutarate_DH_E1. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODO1_BUCAP
AccessionPrimary (citable) accession number: Q8K9N3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents