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Q1RHI5 (ODO2_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 58. 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:RBE_1098
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length400 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 – 400400Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000288095

Regions

Domain1 – 7676Lipoyl-binding

Sites

Active site3711 Potential
Active site3751 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q1RHI5 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 2C8334C1FA6F9A10

FASTA40043,078
        10         20         30         40         50         60 
MGVKIIVPSL GESVTEATIA KWYKKEGDAV KTDELLLEIE TEKVTLEVNS PCNGTIGKII 

        70         80         90        100        110        120 
KADGANVAVG EEIGDINEGE AVATNSNEAA KPQTASQPVP EKVPKKPAVA NNTLAPSVQK 

       130        140        150        160        170        180 
LVTENKLDPN NIKGTGKDGR ITKGDVLETM NAPTPAATST TSSAKASEER VERVRMSRLR 

       190        200        210        220        230        240 
KTIAQRLKDS QNTAAILTTF NEIDMSKVIA LRGKYKDEFE KKHGVKLGFM SFFVRATIEA 

       250        260        270        280        290        300 
LKLIPSVNAE IDGDDLVYKN YYDIGVAVGT EQGLVVPVVR DADKMGFADI EKTIGGLAKK 

       310        320        330        340        350        360 
ARDGKLSMAD LSGGTFSISN GGVYGSLLST PIINPPQSGI LGLHKTEERV VAIDGKIEIR 

       370        380        390        400 
PMMYIALSYD HRIIDGKEAV SFLVKIKELI ESPEKLLLNL 

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000087 Genomic DNA. Translation: ABE05179.1.
RefSeqYP_538268.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RHI5.
SMRQ1RHI5. Positions 172-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336407.RBE_1098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE05179; ABE05179; RBE_1098.
GeneID3995009.
KEGGrbe:RBE_1098.
PATRIC17883773. VBIRicBel102610_1239.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRBEL336407:GJCY-1131-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_RICBR
AccessionPrimary (citable) accession number: Q1RHI5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 16, 2006
Last modified: November 13, 2013
This is version 58 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

Rickettsia bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways