Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6FYD4 (ODO2_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 76. 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:BQ13410
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

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 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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162257

Regions

Domain2 – 7675Lipoyl-binding

Sites

Active site3811 By similarity
Active site3851 By similarity

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Experimental info

Sequence conflict41G → E in AAN78229. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6FYD4 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 216936AE2432DC05

FASTA41043,763
        10         20         30         40         50         60 
MTTGIRVPTL GESVTEATIG KWFKKLGEAV AVDEPLVELE TDKVTVEVPS PVMGKLTEII 

        70         80         90        100        110        120 
AKEGDIVEVN AVLGFVESGA AGISQSFSPS ATSIPEAPSE LEQSPSSSAT PSGTMPPAPS 

       130        140        150        160        170        180 
AAKLMAENNI AKSDISGSGK RGQILKEDVL GALAQGTKAS TSVATLTASS SSAAPIQEMR 

       190        200        210        220        230        240 
EERVRMTKLR QTIARRLKDA QNTAAMLTTF NEVDMSAVMD LRKRYKDLFE KKHGVKLGFM 

       250        260        270        280        290        300 
GFFTKAVCHA LKEFPTVNAE IDGTDIVYKN YVNAGIAVGT DKGLVVPVVR DADQMSLAEI 

       310        320        330        340        350        360 
EKEISRLGRL ARDGKLAVSD MQGGTFTITN GGVYGSLMST PILNAPQSGI LGMHAIKERA 

       370        380        390        400        410 
MVVGGQIIIC PMMYLALSYD HRIVDGQEAV TFLVRVKESL EDPERLVLDL 

« Hide

References

« Hide 'large scale' 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].
Strain: ATCC VR-358 / Fuller / CIP 107027.
[2]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY160680 Genomic DNA. Translation: AAN78229.2.
BX897700 Genomic DNA. Translation: CAF26799.1.
RefSeqYP_032855.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6FYD4.
SMRQ6FYD4. Positions 181-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ13410.

Proteomic databases

PRIDEQ6FYD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF26799; CAF26799; BQ13410.
GeneID2866355.
KEGGbqu:BQ13410.
PATRIC31954159. VBIBarQui58630_1476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
KOK00658.
OMAFEKKHAV.
OrthoDBEOG610413.
ProtClustDBPRK05704.

Enzyme and pathway databases

BioCycBQUI283165:GHZA-1339-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_BARQU
AccessionPrimary (citable) accession number: Q6FYD4
Secondary accession number(s): Q8GCX9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: November 13, 2013
This is version 76 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