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Q8GCY1 (ODO2_BARVB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 61. 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
OrganismBartonella vinsonii subsp. berkhofii
Taxonomic identifier40933 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length411 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 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently.

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 – 411411Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162258

Regions

Domain2 – 7675Lipoyl-binding

Sites

Active site3821 By similarity
Active site3861 By similarity

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q8GCY1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4BE837429BDE913A

FASTA41143,841
        10         20         30         40         50         60 
MTTEIRVPTL GESVTEATVG KWFKKLGEAV AIDEPLVELE TDKVTVEVPS PVAGKLFEII 

        70         80         90        100        110        120 
AKEGDTVEVN ALLGAVEAGA ASVAKSPSSS ETSVSAAPSE LEQSSSSNTM PPAPSAAKLM 

       130        140        150        160        170        180 
AENNIAKSDI LGSGKRGQIL KEDVLNVLAQ GVKTSPPAVS ASSSTPVSVS SSAVAPVQEM 

       190        200        210        220        230        240 
REERVRMTKL RQTIARRLKD AQNTAAMLTT FNEVDMSAVM GLRKRYKDLF EKKHGVKLGF 

       250        260        270        280        290        300 
MGFFTKAVCH ALKELPAVNA EIDGTDIIYK NYVNAGIAVG TDKGLVVPVV RDADQMSLAE 

       310        320        330        340        350        360 
IEKEIGRLGR LARDGKLAVS DMQGGTFTIT NGGVYGSLMS TPILNAPQSG ILGMHAIKER 

       370        380        390        400        410 
AMVVDGQIAI RPMMYLALSY DHRIVDGQEA VTFLVRVKES LEDPERLVLD L 

« Hide

References

[1]"Molecular characterization of the sucB gene encoding the immunogenic dihydrolipoamide succinyltransferase protein of Bartonella vinsonii subsp. berkhoffii and Bartonella quintana."
Gilmore R.D. Jr., Carpio A.M., Kosoy M.Y., Gage K.L.
Infect. Immun. 71:4818-4822(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY160679 Genomic DNA. Translation: AAN78227.1.

3D structure databases

ProteinModelPortalQ8GCY1.
SMRQ8GCY1. Positions 182-411.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.61. 7855.
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_BARVB
AccessionPrimary (citable) accession number: Q8GCY1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: October 16, 2013
This is version 61 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