Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Status
Reviewed-Annotation score: Annotation score: 2 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).UniRule annotation

Catalytic activityi

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.UniRule annotation

Cofactori

thiamine diphosphateUniRule annotation

GO - Molecular functioni

  1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-HAMAP
  2. thiamine pyrophosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
  2. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciSAUR273036:GJVS-1291-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase E1 componentUniRule annotation (EC:1.2.4.2UniRule annotation)
Alternative name(s):
Alpha-ketoglutarate dehydrogenaseUniRule annotation
Gene namesi
Name:odhAUniRule annotation
Ordered Locus Names:SAB1269c
OrganismiStaphylococcus aureus (strain bovine RF122 / ET3-1)
Taxonomic identifieri273036 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001927: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9329322-oxoglutarate dehydrogenase E1 componentPRO_1000065704Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi273036.SAB1269c.

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiEHSNARP.
OrthoDBiEOG6V1M1F.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01169. SucA_OdhA.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR023784. 2oxoglutarate_DH_E1_bac.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2YY05-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND
60 70 80 90 100
DSIVPSLKST SSQNSDGTIK RVMRLIDNIR QYGHLKADIY PVNPPKRKHV
110 120 130 140 150
PKLEIEDFDL DQQTLEGISA GIVSDHFADI YDNAYEAILR MEKRYKGPIA
160 170 180 190 200
FEYTHINNNT ERGWLKRRIE TPYKVTLNNN EKRALFKQLA YVEGFEKYLH
210 220 230 240 250
KNFVGAKRFS IEGVDALVPM LQRTITIAAK EGIKNIQIGM AHRGRLNVLT
260 270 280 290 300
HVLEKPYEMM ISEFMHTDPM KFLPEDGSLQ LTAGWTGDVK YHLGGIKTTD
310 320 330 340 350
SYGTMQRIAL ANNPSHLEIV APVVEGRTRA AQDDTQRAGA PTTDHHKAMP
360 370 380 390 400
IIIHGDGAYP GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA
410 420 430 440 450
RSTTYSTDVA KGYDVPIFHV NADDVEATIE AIDIAMEFRK EFHKDVVIDL
460 470 480 490 500
VGYRRFGHNE MDEPSITNPV PYQNIRKNDS VEYVFGKKLV NEGVISEDEM
510 520 530 540 550
HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPAELALPLQ ADEQSFTFDH
560 570 580 590 600
LKEINDALLT YPDGFNILKK LNKVLKKRHE PFNKEDGLVD WAQAEQLAFA
610 620 630 640 650
TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPNQKATF
660 670 680 690 700
DIHNSPLSEA AVVGFEYGYN VENKKSFNIW EAQYGDFANM SQMIFDNFLF
710 720 730 740 750
SSRSKWGERS GLTLFLPHAY EGQGPEHSSA RLERFLQLAA ENNCTVVNLS
760 770 780 790 800
SSSNYFHLLR AQAASLDSEQ MRPLVVMSPK SLLRNKTVAK PIDEFTSGGF
810 820 830 840 850
EPILTESYQA DKVTKVILAT GKMFIDLKEA LAKNPDESVL LVAIERLYPF
860 870 880 890 900
PEEEIETLLA QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY
910 920 930
HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN
Length:932
Mass (Da):105,364
Last modified:December 20, 2005 - v1
Checksum:iA8642ACB91D4A5B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI80958.1.
RefSeqiYP_416746.1. NC_007622.1.

Genome annotation databases

EnsemblBacteriaiCAI80958; CAI80958; SAB1269c.
GeneIDi3793631.
KEGGisab:SAB1269c.
PATRICi19523409. VBIStaAur92441_1353.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI80958.1.
RefSeqiYP_416746.1. NC_007622.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273036.SAB1269c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI80958; CAI80958; SAB1269c.
GeneIDi3793631.
KEGGisab:SAB1269c.
PATRICi19523409. VBIStaAur92441_1353.

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiEHSNARP.
OrthoDBiEOG6V1M1F.

Enzyme and pathway databases

BioCyciSAUR273036:GJVS-1291-MONOMER.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
HAMAPiMF_01169. SucA_OdhA.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR023784. 2oxoglutarate_DH_E1_bac.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.
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 nameiODO1_STAAB
AccessioniPrimary (citable) accession number: Q2YY05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 20, 2005
Last modified: February 4, 2015
This is version 72 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. 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.