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Q89AJ6 (ODO2_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 86. 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:
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:bbp_281
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length410 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 – 410410Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162261

Regions

Domain1 – 7777Lipoyl-binding

Sites

Active site3811 Potential
Active site3851 Potential

Amino acid modifications

Modified residue441N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q89AJ6 [UniParc].

Last modified June 16, 2003. Version 1.
Checksum: 224A816E151499B0

FASTA41046,543
        10         20         30         40         50         60 
MNIINIFIPD LPESVTDATI IKWHKKKGDK VQEDTILVDI ETDKVILEIP SPSDGILNSI 

        70         80         90        100        110        120 
IADKGKIVLP GQVIGTLLKI GIKNEEKIIK TTNNVVNTDN NQNINLKLLE KTYSPTVRRL 

       130        140        150        160        170        180 
ISMHDLRDVD IIQGTGTKNR LTRKDILNYL KNIRSNTNKK INNYDLNAYN FNTTHKNHRS 

       190        200        210        220        230        240 
IKRVKMTRLR KKISERLLST KNNTASLTTF NEVNMQSILN LRRKYGELFK QKHGIKLGLM 

       250        260        270        280        290        300 
SFYVKAVIEA LKIFPEINAS IDNDEIIYYN YFDISIAIST PRGLVTPVLK NADLMSMAEI 

       310        320        330        340        350        360 
EIKIKDFSEK GKNSKLTIDD LIGGNFTITN GGVFGSLFST PLINPPQSAI LGMHAIHKRP 

       370        380        390        400        410 
VIVDENIEVH PMMYLALSYD HRLIDGKESV GFLLKIKEFL EDFSRIVLNI 

« 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: AAO27006.1.
RefSeqNP_777901.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AJ6.
SMRQ89AJ6. Positions 179-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO27006; AAO27006; bbp_281.
GeneID1058259.
KEGGbab:bbp281.
PATRIC21245349. VBIBucAph80364_0277.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
KOK00658.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-281-MONOMER.
UniPathwayUPA00868; UER00840.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODO2_BUCBP
AccessionPrimary (citable) accession number: Q89AJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 16, 2003
Last modified: November 13, 2013
This is version 86 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