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Q8K9N2 (ODO2_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

EC=2.3.1.61
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name=OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene names
Name:sucB
Ordered Locus Names:BUsg_293
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length393 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

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162260

Regions

Domain1 – 7777Lipoyl-binding

Sites

Active site3641 Potential
Active site3681 Potential

Amino acid modifications

Modified residue441N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q8K9N2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 567682324ED9361D

FASTA39345,154
        10         20         30         40         50         60 
MNRINILVPD LPESVNDAVV VKWYKKIGEQ ISSEDNIVDI ETDKVMLEVS APCNGILNEI 

        70         80         90        100        110        120 
LEKEGSIVKS NQILGNIVES KNIESKTKSK LEKSNKYFIK DKNFNISFKE KIYNFPPSIR 

       130        140        150        160        170        180 
RIIRIKKNKE IFNELNYIKN QENIIEEKLN DQSFSNEKEK KIYENRIKMT RLRQKIAERL 

       190        200        210        220        230        240 
LETKNNTAML TTFNEVNMQP IISLRKKYGE FFEKKHGVRI GFMPFFVKAV VESLKKFPEI 

       250        260        270        280        290        300 
NASIDKNDIV YYKNIDVSIA VSTPRGVITP VLRNADNMSM ADIEKKIKEF SIKGIENKIK 

       310        320        330        340        350        360 
IEELIGGNFT ITNGGIFGSL MSTPIINPPQ SAILGMHLIK ERPMAINGKV KILPMMYLAL 

       370        380        390 
SYDHRLIDGK ESVSFLVTIK NILEDFNRII INV 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67848.1.
RefSeqNP_660637.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9N2.
SMRQ8K9N2. Positions 164-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67848; AAM67848; BUsg_293.
GeneID1005497.
KEGGbas:BUsg293.
PATRIC21247395. VBIBucAph100086_0307.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
KOK00658.
OMASEIHAPE.
OrthoDBEOG610413.
ProtClustDBCLSK315790.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-307-MONOMER.
UniPathwayUPA00868; UER00840.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
InterProIPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODO2_BUCAP
AccessionPrimary (citable) accession number: Q8K9N2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 82 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Buchnera aphidicola (subsp. Schizaphis graminum)

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