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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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

BioCyciSAUR158879:GJCB-1312-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:SA1245
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9109102-oxoglutarate dehydrogenase E1 componentPRO_0000162178Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi158879.SA1245.

Structurei

3D structure databases

ProteinModelPortaliQ99U74.
ModBaseiSearch...
MobiDBiSearch...

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.

Q99U74-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNERKEVSE APVNFGANLG LMLDLYDDFL QDPSSVPEDL QVLFSTIKRV
60 70 80 90 100
MRLIDNIRQY GHLKADIYPV NPPKRKHVPK LEIEDFDLDQ QTLEGISAGI
110 120 130 140 150
VSDHFADIYD NAYEAILRME KRYKGPIAFE YTHINNNTER GWLKRRIETP
160 170 180 190 200
YKVTLNNNEK RALFKQLAYV EGFEKYLHKN FVGAKRFSIE GVDALVPMLQ
210 220 230 240 250
RTITIAAKEG IKNIQIGMAH RGRLNVLTHV LEKPYEMMIS EFMHTDPMKF
260 270 280 290 300
LPEDGSLQLT AGWTGDVKYH LGGIKTTDSY GTMQRIALAN NPSHLEIVAP
310 320 330 340 350
VVEGRTRAAQ DDTQRAGAPT TDHHKAMPII IHGDAAYPGQ GINFETMNLG
360 370 380 390 400
NLKGYSTGGS LHIITNNRIG FTTEPIDARS TTYSTDVAKG YDVPIFHVNA
410 420 430 440 450
DDVEATIEAI DIAMEFRKEF HKDVVIDLVG YRRFGHNEMD EPSITNPVPY
460 470 480 490 500
QNIRKHDSVE YVFGKKLVNE GVISEDEMHS FIEQVQKELR QAHDKINKAD
510 520 530 540 550
KMDNPDMEKP AELALPLQAD EQSFTFDHLK EINDALLTYP DGFNILKKLN
560 570 580 590 600
KVLEKRHEPF NKEDGLVDWA QAEQLAFATI LQDGTPIRLT GQDSERGTFS
610 620 630 640 650
HRHAVLHDEQ TGETYTPLHH VPDQKATFDI HNSPLSEAAV VGFEYGYNVE
660 670 680 690 700
NKKSFNIWEA QYGDFANMSQ MIFDNFLFSS RSKWGERSGL TLFLPHAYEG
710 720 730 740 750
QGPEHSSARL ERFLQLAAEN NCTVVNLSSS SNYFHLLRAQ AASLDSEQMR
760 770 780 790 800
PLVVMSPKSL LRNKTVAKPI DEFTSGGFEP ILTESYQADK VTKVILATGK
810 820 830 840 850
MFIDLKEALA KNPDESVLLV AIERLYPFPE EEIEALLAQL PKLEEVSWVQ
860 870 880 890 900
EEPKNQGAWL YVYPYVKVLV ADKYDLSYHG RIQRAAPAEG DGEIHKLVQN
910
KIIENALKNN
Length:910
Mass (Da):103,112
Last modified:June 1, 2001 - v1
Checksum:i7803AAED537CF247
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42505.1.
PIRiE89918.
RefSeqiNP_374526.1. NC_002745.2.
WP_000180688.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42505; BAB42505; BAB42505.
KEGGisau:SA1245.
PATRICi19574740. VBIStaAur116463_1339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42505.1.
PIRiE89918.
RefSeqiNP_374526.1. NC_002745.2.
WP_000180688.1. NC_002745.2.

3D structure databases

ProteinModelPortaliQ99U74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158879.SA1245.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB42505; BAB42505; BAB42505.
KEGGisau:SA1245.
PATRICi19574740. VBIStaAur116463_1339.

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiEHSNARP.
OrthoDBiEOG6V1M1F.

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1312-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.
  2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiODO1_STAAN
AccessioniPrimary (citable) accession number: Q99U74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 82 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.