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Q9ZDY4 (ODO2_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:RP179
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length401 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162269

Regions

Domain1 – 7676Lipoyl-binding

Sites

Active site3721 Potential
Active site3761 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZDY4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 353F81339C5E9F23

FASTA40143,979
        10         20         30         40         50         60 
MSVKIIIPSL GESVTEATIA KWYKKLGDSV KTDELLLEIE TEKVTLEVNA PCNGTIEKIA 

        70         80         90        100        110        120 
KTDGANVTVG EEIGEINEVV DTDTACTNNN SYKKQAIVQH DSEQIVDKPA SSSNILAPSV 

       130        140        150        160        170        180 
QKLVTENKLD PNNIKGTGRG GRITKCDVLE TINTTPVTIE TPALNKTNEE RTQRVRMSRL 

       190        200        210        220        230        240 
RKTIAQRLKD SQNTAAILTT FNEIDMSKVI ALRNQYKEEF EKKHTVKLGF MSFFVKATIE 

       250        260        270        280        290        300 
ALKLIPSINA EIDGDDLLYK NYYDIGVAVG TDQGLVVPVV RDADKMGFAD VEQAIGDLAK 

       310        320        330        340        350        360 
KAREGKLSMS DLSGGTFSIS NGGVYGSLLS TPIINPPQSG ILGLHKTEER AVVIDGKIEI 

       370        380        390        400 
RPMMYIALSY DHRIIDGKEG VSFLVKIKNL IENPEKLLLN L 

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235270 Genomic DNA. Translation: CAA14646.1.
PIRG71728.
RefSeqNP_220569.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZDY4.
SMRQ9ZDY4. Positions 174-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA14646; CAA14646; CAA14646.
GeneID883874.
KEGGrpr:RP179.
PATRIC17901108. VBIRicPro72556_0184.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
KOK00658.
OMAMMSTPIV.
OrthoDBEOG610413.

Enzyme and pathway databases

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_RICPR
AccessionPrimary (citable) accession number: Q9ZDY4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 95 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 prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways