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Protein

2-oxoglutarate dehydrogenase E1 component

Gene

odhA

Organism
Staphylococcus haemolyticus (strain JCSC1435)
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

BioCyciSHAE279808:GJX7-1546-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:SH1492
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9349342-oxoglutarate dehydrogenase E1 componentPRO_0000162184Add
BLAST

Proteomic databases

PRIDEiQ4L6C4.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi279808.SH1492.

Structurei

3D structure databases

ProteinModelPortaliQ4L6C4.
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.

Q4L6C4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKDNKDVTE APVNFGANLG LMLDLYDDYL QDPSSVPDDL QVLFSTIKNG
60 70 80 90 100
EAHVAAKSTT EGSGSSAGDG TIKRIMRLID NIRQYGHLKA DIYPVNAPKR
110 120 130 140 150
TNLPKLEIEE FNLDKETLEN VSAEIVSDHF KDIYDNAYEA IERMEKRYKG
160 170 180 190 200
PIAFEYNHIN NNKERTWLKR RIETPYRANI NNDERKKLFD TLAHVEGFEK
210 220 230 240 250
YLHKNFVGAK RFSIEGVDTL VPMLQHTLKR AAEIEINNIQ IGMAHRGRLN
260 270 280 290 300
VLTHVLEKPY EMMISEFMHT DPMKFLPEDG SLELTAGWTG DVKYHLGGVK
310 320 330 340 350
TTSSYGIEQR ISLANNPSHL EIVAPVVIGK TRASQDDTKH AGKPTTDFHK
360 370 380 390 400
GMPIIIHGDA AYPGQGINFE TMNLSNLDGY STGGALHIIT NNRIGFTTEP
410 420 430 440 450
VDGRSTTYST DIAKGYDVPI LHVNADDVEA TIEAIDIAME FRKEFHKDFV
460 470 480 490 500
IDLVGYRRYG HNEMDEPSIT NPLPYHNIRK HDSVEIIYGN KLVEDGVISK
510 520 530 540 550
EQMEDVMDKV QKEMRAAQDK IDKSDKMDNP DMERPESLQE PLQSDDKDFS
560 570 580 590 600
VDHLKEINDA MLTYPEDFHV LKKLNKVLEK RREPFESENG LVDWAQAEQL
610 620 630 640 650
AFATIVQDGI SVRLTGQDSE RGTFSHRHAV LHDEENGDTF TPLHHVPNQK
660 670 680 690 700
ATFEVHNSPL SEAAVVGFEY GYNVENKNSM NIWEAQYGDF SNMAQMMFDN
710 720 730 740 750
FMSSARAKWG ERSGLTLFLP HAFEGQGPEH SSARLERFLQ LAAENNSTVV
760 770 780 790 800
NLSSSSNYFH LLRAQAKSLG TEAMRPLIVM SPKSLLRNKT VAKPIDQFTS
810 820 830 840 850
GGFKPIIVED GNKEKVTKLV LASGKMFIDL KEHLAKNPDD SILLVAVDRL
860 870 880 890 900
YPFPEGEIKE VLNELPNLET VSWVQEEPKN QGAWLFVYPY LKSLVGNQFN
910 920 930
LSYHGRIQRA APAEGDGEIH KLVQNQIIES SIEK
Length:934
Mass (Da):105,479
Last modified:August 2, 2005 - v1
Checksum:i7D9E801A49E880E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE04801.1.
RefSeqiWP_011275787.1. NC_007168.1.
YP_253407.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE04801; BAE04801; SH1492.
GeneIDi3481998.
KEGGisha:SH1492.
PATRICi19619095. VBIStaHae67511_1471.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE04801.1.
RefSeqiWP_011275787.1. NC_007168.1.
YP_253407.1. NC_007168.1.

3D structure databases

ProteinModelPortaliQ4L6C4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279808.SH1492.

Proteomic databases

PRIDEiQ4L6C4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE04801; BAE04801; SH1492.
GeneIDi3481998.
KEGGisha:SH1492.
PATRICi19619095. VBIStaHae67511_1471.

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259588.
KOiK00164.
OMAiEHSNARP.
OrthoDBiEOG6V1M1F.

Enzyme and pathway databases

BioCyciSHAE279808:GJX7-1546-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. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiODO1_STAHJ
AccessioniPrimary (citable) accession number: Q4L6C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: August 2, 2005
Last modified: February 4, 2015
This is version 70 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.