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Q68XI8 (ODO2_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 69. 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:RT0170
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length398 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 – 398398Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000288097

Regions

Domain1 – 7676Lipoyl-binding

Sites

Active site3691 Potential
Active site3731 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q68XI8 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 76C55B5C51446A98

FASTA39843,823
        10         20         30         40         50         60 
MSIKIIIPSL GESVTEATIA KWYKKLGDAV KTDELLLEIE TDKVTLEVNA PCNGTIGKIS 

        70         80         90        100        110        120 
KTDGANVTVG EEVGEINEIA DTDTAWINNK KQEVSQHTSE QLVDKPAMAS NILAPSVQKL 

       130        140        150        160        170        180 
VTENKLDPNN IKGTGRGGRI TKYDVLETIN TTPITIETHA INKTNEERTQ RVRMSRLRKT 

       190        200        210        220        230        240 
IAQRLKDSQN TAAILTTFNE IDMSKVIALR NQYKEEFEKK HTVKLGFMSF FVKATIEALK 

       250        260        270        280        290        300 
LIPSINAEID GDDLLYKNYY DIGVAVGTEQ GLVVPVIRDA DKMSFADIEQ AIGNLAKKAR 

       310        320        330        340        350        360 
EGKLSISDLS GGTFSISNGG VYGSLLSTPI INPPQSGILG LHKTEERAVV IDGKIEIRPM 

       370        380        390 
MYIALSYDHR IIDGKEGVSF LVKIKNLIEN PEKLLLNL 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU03654.1.
RefSeqYP_067136.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68XI8.
SMRQ68XI8. Positions 171-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257363.RT0170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU03654; AAU03654; RT0170.
GeneID2959241.
KEGGrty:RT0170.
PATRIC17909514. VBIRicTyp34752_0176.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
KOK00658.
OMADMAGATF.
OrthoDBEOG610413.
ProtClustDBPRK05704.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-179-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_RICTY
AccessionPrimary (citable) accession number: Q68XI8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2004
Last modified: November 13, 2013
This is version 69 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 typhi

Rickettsia typhi (strain Wilmington): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways