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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

odhB

Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei393 – 3931By similarity
Active sitei397 – 3971By similarity

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciSAUR273036:GJVS-1290-MONOMER.
UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:odhB
Ordered Locus Names:SAB1268c
OrganismiStaphylococcus aureus (strain bovine RF122 / ET3-1)
Taxonomic identifieri273036 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001927 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000288098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-lipoyllysinePROSITE-ProRule annotation

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

Protein-protein interaction databases

STRINGi273036.SAB1268c.

Structurei

3D structure databases

ProteinModelPortaliQ2YY06.
SMRiQ2YY06. Positions 193-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiTFGKKAR.
OrthoDBiEOG610413.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2YY06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE
60 70 80 90 100
EAGVLSEQLA SEGDTVEVGQ AIAVIGEGSG NASKENSNDN TPQQNEETNN
110 120 130 140 150
KKEETTNKSA DNAEVNQTND YNQQRVNATP SARRYARENG VNLAEVSPKT
160 170 180 190 200
NDVVRKEDID KKQQAPASTQ TTQQAPAKEE KKYNQYPTKP VIREKMSRRK
210 220 230 240 250
KTAAKKLLEV SNNTAMLTTF NEVDMTNVME LRKRKKEQFM KDHDGTKLGF
260 270 280 290 300
MSFFTKASVA ALKKYPEVNA EIDGDDMITK QYYDIGVAVS TDDGLLVPFV
310 320 330 340 350
RDCDKKNFAE IEAEIANLAV KAREKKLGLD DMVNGSFTIT NGGIFGSMMS
360 370 380 390 400
TPIINGNQAA ILGMHSIITR PIAIDQDTIE NRPMMYIALS YDHRIIDGKE
410 420
AVGFLKTIKE LIENPEDLLL ES
Length:422
Mass (Da):46,705
Last modified:December 20, 2005 - v1
Checksum:iF45D1227F4EC0C95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI80957.1.
RefSeqiWP_001115457.1. NC_007622.1.
YP_416745.1. NC_007622.1.

Genome annotation databases

EnsemblBacteriaiCAI80957; CAI80957; SAB1268c.
KEGGisab:SAB1268c.
PATRICi19523407. VBIStaAur92441_1352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI80957.1.
RefSeqiWP_001115457.1. NC_007622.1.
YP_416745.1. NC_007622.1.

3D structure databases

ProteinModelPortaliQ2YY06.
SMRiQ2YY06. Positions 193-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273036.SAB1268c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI80957; CAI80957; SAB1268c.
KEGGisab:SAB1268c.
PATRICi19523407. VBIStaAur92441_1352.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiTFGKKAR.
OrthoDBiEOG610413.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
BioCyciSAUR273036:GJVS-1290-MONOMER.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular correlates of host specialization in Staphylococcus aureus."
    Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
    PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: bovine RF122 / ET3-1.

Entry informationi

Entry nameiODO2_STAAB
AccessioniPrimary (citable) accession number: Q2YY06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: December 20, 2005
Last modified: April 29, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.