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P57389 (ODO2_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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:BU303
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length420 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162259

Regions

Domain1 – 7777Lipoyl-binding

Sites

Active site3911 Potential
Active site3951 Potential

Amino acid modifications

Modified residue441N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
P57389 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: E0028D647A5CE34C

FASTA42048,092
        10         20         30         40         50         60 
MKKINILVPD LPESISDATV VKWHKKIGDT VHCDDNIVDI ETDKVMLEVS SPCDGILQSI 

        70         80         90        100        110        120 
LEKEGKVVIS QQTLGEINKS TVVDNHLSNN HIIEKEDNLL KKEEKYITTE EKKEIEYLLK 

       130        140        150        160        170        180 
DNHKHLTPSM RRSVKIHNIN NGFLNQVIET SKKTNFENII KEEKKESNQI LFNHNIFNAN 

       190        200        210        220        230        240 
ENNKNNNNKV TNRVKMTRLR QRIAERLLDS KNNTAMLTTF HEVNMKPIIL LRKKYGEDFE 

       250        260        270        280        290        300 
KKHNVRIGFM SFFVKAVIQA LKNFPEINAY IDQTDIVFYK NFDISIAIST PRGLITPVIR 

       310        320        330        340        350        360 
NADTMTMAEI EKKIKDFSIK GLQNKINIKE LMGGNFTITN GGVFGSLMST PIINPPQTAI 

       370        380        390        400        410        420 
LGMHVIQERP VVVNGQIKIL PMMYLALSYD HRLIDGKESV GFLINIKNIL EDFNRIAIDV 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB13012.1.
RefSeqNP_240126.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57389.
SMRP57389. Positions 193-420.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB13012; BAB13012; BAB13012.
GeneID1110002.
KEGGbuc:BU303.
PATRIC21244132. VBIBucAph127364_0314.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
KOK00658.
OMASEIHAPE.
OrthoDBEOG610413.
ProtClustDBCLSK315790.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-303-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_BUCAI
AccessionPrimary (citable) accession number: P57389
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 19, 2014
This is version 88 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. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names