Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2YY05 (ODO1_STAAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
2-oxoglutarate dehydrogenase E1 component

EC=1.2.4.2
Alternative name(s):
Alpha-ketoglutarate dehydrogenase
Gene names
Name:odhA
Ordered Locus Names:SAB1269c
OrganismStaphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]
Taxonomic identifier273036 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length932 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. HAMAP-Rule MF_01169

Catalytic activity

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. HAMAP-Rule MF_01169

Cofactor

Thiamine pyrophosphate By similarity. HAMAP-Rule MF_01169

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01169

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandThiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: InterPro

   Molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

thiamine pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9329322-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169
PRO_1000065704

Sequences

Sequence LengthMass (Da)Tools
Q2YY05 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: A8642ACB91D4A5B0

FASTA932105,364
        10         20         30         40         50         60 
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND DSIVPSLKST 

        70         80         90        100        110        120 
SSQNSDGTIK RVMRLIDNIR QYGHLKADIY PVNPPKRKHV PKLEIEDFDL DQQTLEGISA 

       130        140        150        160        170        180 
GIVSDHFADI YDNAYEAILR MEKRYKGPIA FEYTHINNNT ERGWLKRRIE TPYKVTLNNN 

       190        200        210        220        230        240 
EKRALFKQLA YVEGFEKYLH KNFVGAKRFS IEGVDALVPM LQRTITIAAK EGIKNIQIGM 

       250        260        270        280        290        300 
AHRGRLNVLT HVLEKPYEMM ISEFMHTDPM KFLPEDGSLQ LTAGWTGDVK YHLGGIKTTD 

       310        320        330        340        350        360 
SYGTMQRIAL ANNPSHLEIV APVVEGRTRA AQDDTQRAGA PTTDHHKAMP IIIHGDGAYP 

       370        380        390        400        410        420 
GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA RSTTYSTDVA KGYDVPIFHV 

       430        440        450        460        470        480 
NADDVEATIE AIDIAMEFRK EFHKDVVIDL VGYRRFGHNE MDEPSITNPV PYQNIRKNDS 

       490        500        510        520        530        540 
VEYVFGKKLV NEGVISEDEM HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPAELALPLQ 

       550        560        570        580        590        600 
ADEQSFTFDH LKEINDALLT YPDGFNILKK LNKVLKKRHE PFNKEDGLVD WAQAEQLAFA 

       610        620        630        640        650        660 
TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPNQKATF DIHNSPLSEA 

       670        680        690        700        710        720 
AVVGFEYGYN VENKKSFNIW EAQYGDFANM SQMIFDNFLF SSRSKWGERS GLTLFLPHAY 

       730        740        750        760        770        780 
EGQGPEHSSA RLERFLQLAA ENNCTVVNLS SSSNYFHLLR AQAASLDSEQ MRPLVVMSPK 

       790        800        810        820        830        840 
SLLRNKTVAK PIDEFTSGGF EPILTESYQA DKVTKVILAT GKMFIDLKEA LAKNPDESVL 

       850        860        870        880        890        900 
LVAIERLYPF PEEEIETLLA QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY 

       910        920        930 
HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ938182 Genomic DNA. Translation: CAI80958.1.
RefSeqYP_416746.1. NC_007622.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273036.SAB1269c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI80958; CAI80958; SAB1269c.
GeneID3793631.
KEGGsab:SAB1269c.
PATRIC19523409. VBIStaAur92441_1353.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0567.
HOGENOMHOG000259588.
KOK00164.
OMANEGVANE.
OrthoDBEOG6V1M1F.
ProtClustDBPRK09404.

Enzyme and pathway databases

BioCycSAUR273036:GJVS-1291-MONOMER.

Family and domain databases

HAMAPMF_01169. SucA_OdhA.
InterProIPR011603. 2oxoglutarate_DH_E1.
IPR023784. 2oxoglutarate_DH_E1_bac.
IPR001017. DH_E1.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODO1_STAAB
AccessionPrimary (citable) accession number: Q2YY05
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 20, 2005
Last modified: February 19, 2014
This is version 65 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