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Q2YY06

- ODO2_STAAB

UniProt

Q2YY06 - ODO2_STAAB

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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene
odhB, SAB1268c
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei393 – 3931 By similarity
Active sitei397 – 3971 By 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: 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-lipoyllysine Reviewed prediction

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7574Lipoyl-bindingAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
KOiK00658.
OMAiSMAESIT.
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

MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE    50
EAGVLSEQLA SEGDTVEVGQ AIAVIGEGSG NASKENSNDN TPQQNEETNN 100
KKEETTNKSA DNAEVNQTND YNQQRVNATP SARRYARENG VNLAEVSPKT 150
NDVVRKEDID KKQQAPASTQ TTQQAPAKEE KKYNQYPTKP VIREKMSRRK 200
KTAAKKLLEV SNNTAMLTTF NEVDMTNVME LRKRKKEQFM KDHDGTKLGF 250
MSFFTKASVA ALKKYPEVNA EIDGDDMITK QYYDIGVAVS TDDGLLVPFV 300
RDCDKKNFAE IEAEIANLAV KAREKKLGLD DMVNGSFTIT NGGIFGSMMS 350
TPIINGNQAA ILGMHSIITR PIAIDQDTIE NRPMMYIALS YDHRIIDGKE 400
AVGFLKTIKE LIENPEDLLL ES 422
Length:422
Mass (Da):46,705
Last modified:December 20, 2005 - v1
Checksum:iF45D1227F4EC0C95
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ938182 Genomic DNA. Translation: CAI80957.1.
RefSeqiYP_416745.1. NC_007622.1.

Genome annotation databases

EnsemblBacteriaiCAI80957; CAI80957; SAB1268c.
GeneIDi3793632.
KEGGisab:SAB1268c.
PATRICi19523407. VBIStaAur92441_1352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ938182 Genomic DNA. Translation: CAI80957.1 .
RefSeqi YP_416745.1. NC_007622.1.

3D structure databases

ProteinModelPortali Q2YY06.
SMRi Q2YY06. Positions 193-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273036.SAB1268c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAI80957 ; CAI80957 ; SAB1268c .
GeneIDi 3793632.
KEGGi sab:SAB1268c.
PATRICi 19523407. VBIStaAur92441_1352.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281563.
KOi K00658.
OMAi SMAESIT.
OrthoDBi EOG610413.

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .
BioCyci SAUR273036:GJVS-1290-MONOMER.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01347. sucB. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 68 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

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