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Q4L6C4 (ODO1_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:SH1492
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length934 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 – 9349342-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169
PRO_0000162184

Sequences

Sequence LengthMass (Da)Tools
Q4L6C4 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 7D9E801A49E880E9

FASTA934105,479
        10         20         30         40         50         60 
MAKDNKDVTE APVNFGANLG LMLDLYDDYL QDPSSVPDDL QVLFSTIKNG EAHVAAKSTT 

        70         80         90        100        110        120 
EGSGSSAGDG TIKRIMRLID NIRQYGHLKA DIYPVNAPKR TNLPKLEIEE FNLDKETLEN 

       130        140        150        160        170        180 
VSAEIVSDHF KDIYDNAYEA IERMEKRYKG PIAFEYNHIN NNKERTWLKR RIETPYRANI 

       190        200        210        220        230        240 
NNDERKKLFD TLAHVEGFEK YLHKNFVGAK RFSIEGVDTL VPMLQHTLKR AAEIEINNIQ 

       250        260        270        280        290        300 
IGMAHRGRLN VLTHVLEKPY EMMISEFMHT DPMKFLPEDG SLELTAGWTG DVKYHLGGVK 

       310        320        330        340        350        360 
TTSSYGIEQR ISLANNPSHL EIVAPVVIGK TRASQDDTKH AGKPTTDFHK GMPIIIHGDA 

       370        380        390        400        410        420 
AYPGQGINFE TMNLSNLDGY STGGALHIIT NNRIGFTTEP VDGRSTTYST DIAKGYDVPI 

       430        440        450        460        470        480 
LHVNADDVEA TIEAIDIAME FRKEFHKDFV IDLVGYRRYG HNEMDEPSIT NPLPYHNIRK 

       490        500        510        520        530        540 
HDSVEIIYGN KLVEDGVISK EQMEDVMDKV QKEMRAAQDK IDKSDKMDNP DMERPESLQE 

       550        560        570        580        590        600 
PLQSDDKDFS VDHLKEINDA MLTYPEDFHV LKKLNKVLEK RREPFESENG LVDWAQAEQL 

       610        620        630        640        650        660 
AFATIVQDGI SVRLTGQDSE RGTFSHRHAV LHDEENGDTF TPLHHVPNQK ATFEVHNSPL 

       670        680        690        700        710        720 
SEAAVVGFEY GYNVENKNSM NIWEAQYGDF SNMAQMMFDN FMSSARAKWG ERSGLTLFLP 

       730        740        750        760        770        780 
HAFEGQGPEH SSARLERFLQ LAAENNSTVV NLSSSSNYFH LLRAQAKSLG TEAMRPLIVM 

       790        800        810        820        830        840 
SPKSLLRNKT VAKPIDQFTS GGFKPIIVED GNKEKVTKLV LASGKMFIDL KEHLAKNPDD 

       850        860        870        880        890        900 
SILLVAVDRL YPFPEGEIKE VLNELPNLET VSWVQEEPKN QGAWLFVYPY LKSLVGNQFN 

       910        920        930 
LSYHGRIQRA APAEGDGEIH KLVQNQIIES SIEK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE04801.1.
RefSeqYP_253407.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L6C4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH1492.

Proteomic databases

PRIDEQ4L6C4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE04801; BAE04801; SH1492.
GeneID3481998.
KEGGsha:SH1492.
PATRIC19619095. VBIStaHae67511_1471.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0567.
HOGENOMHOG000259588.
KOK00164.
OMAEMDEPST.
OrthoDBEOG6V1M1F.
ProtClustDBPRK09404.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-1546-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_STAHJ
AccessionPrimary (citable) accession number: Q4L6C4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: August 2, 2005
Last modified: February 19, 2014
This is version 63 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