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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus aureus (strain COL)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciSAUR93062:GCEP-1424-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:SACOL1449
OrganismiStaphylococcus aureus (strain COL)
Taxonomic identifieri93062 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000530 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9329322-oxoglutarate dehydrogenase E1 componentPRO_0000162176Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi93062.SACOL1449.

Structurei

3D structure databases

ProteinModelPortaliQ5HG06.
SMRiQ5HG06. Positions 71-929.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiQNQGAWF.
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.

Q5HG06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKND
60 70 80 90 100
DSIVPALKST 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
IIIHGDAAYP GQGINFETMN LGNLKGYSTG GSLHIITNNR IGFTTEPIDA
410 420 430 440 450
RSTTYSTDVA KGYDVPIFHV NADDVEATIE AIDIAMEFRK EFHKDVVIDL
460 470 480 490 500
VGYRRFGHNE MDEPSITNPV PYQNIRKHDS VEYVFGKKLV NEGVISEDEM
510 520 530 540 550
HSFIEQVQKE LRQAHDKINK ADKMDNPDME KPADLALPLQ ADEQSFTFDH
560 570 580 590 600
LKEINDALLT YPDGFNILKK LNKVLEKRHE PFNKEDGLVD WAQAEQLAFA
610 620 630 640 650
TILQDGTPIR LTGQDSERGT FSHRHAVLHD EQTGETYTPL HHVPDQKATF
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
PEEEIEALLA QLPNLEEVSW VQEEPKNQGA WLYVYPYVKV LVADKYDLSY
910 920 930
HGRIQRAAPA EGDGEIHKLV QNKIIENALK NN
Length:932
Mass (Da):105,343
Last modified:February 15, 2005 - v1
Checksum:iB81FAF6A0FA6A4F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW38194.1.
RefSeqiWP_000180666.1. NC_002951.2.

Genome annotation databases

EnsemblBacteriaiAAW38194; AAW38194; SACOL1449.
GeneIDi23197224.
KEGGisac:SACOL1449.
PATRICi19529119. VBIStaAur112458_1413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW38194.1.
RefSeqiWP_000180666.1. NC_002951.2.

3D structure databases

ProteinModelPortaliQ5HG06.
SMRiQ5HG06. Positions 71-929.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1449.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW38194; AAW38194; SACOL1449.
GeneIDi23197224.
KEGGisac:SACOL1449.
PATRICi19529119. VBIStaAur112458_1413.

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiQNQGAWF.
OrthoDBiEOG6V1M1F.

Enzyme and pathway databases

BioCyciSAUR93062:GCEP-1424-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. "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
    Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.
    , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
    J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: COL.

Entry informationi

Entry nameiODO1_STAAC
AccessioniPrimary (citable) accession number: Q5HG06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: February 15, 2005
Last modified: July 22, 2015
This is version 74 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.