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Q4L6C3 (ODO2_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:odhB
Synonyms:sucB
Ordered Locus Names:SH1493
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length423 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 – 423423Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000288109

Regions

Domain2 – 7574Lipoyl-binding

Sites

Active site3941 By similarity
Active site3981 By similarity

Amino acid modifications

Modified residue421N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q4L6C3 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: C1FD7CF93C4E1D88

FASTA42346,249
        10         20         30         40         50         60 
MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE EEGVLQEQLA 

        70         80         90        100        110        120 
SEGDTVEVGQ VIATVGEGSG NASSSKEESS DQSQSANNDE ATKELAQPTE SQSNNEETQS 

       130        140        150        160        170        180 
NPNNQRVNAT PSARRHAREN GVDLSTVSGK GNDVVRKDDV ENSQKAAQSQ SSQETSKKEE 

       190        200        210        220        230        240 
PKKSSGAPNK PVIREKMSRR KKTAAKKLLE VSNNTAMLTT FNEVDMTNVM ELRKRKKEQF 

       250        260        270        280        290        300 
IKDHDGTKLG FMSFFTKAAV AALKKYPEVN AEIDGDDMIT KQYYDIGVAV STDDGLLVPF 

       310        320        330        340        350        360 
VRDCDKKNFA ELERAIADLA VKARDKKLGL DDMVNGSFTI TNGGVFGSMM STPIINGNQA 

       370        380        390        400        410        420 
AILGMHSIIT RPIAIDKDTI ENRPMMYIAL SYDHRIIDGK EAVGFLKTIK ELIESPEDLL 


LES 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE04802.1.
RefSeqYP_253408.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L6C3.
SMRQ4L6C3. Positions 194-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH1493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE04802; BAE04802; SH1493.
GeneID3481999.
KEGGsha:SH1493.
PATRIC19619097. VBIStaHae67511_1472.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
KOK00658.
OMAQEDETVE.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-1547-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_STAHJ
AccessionPrimary (citable) accession number: Q4L6C3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: August 2, 2005
Last modified: May 14, 2014
This is version 70 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