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C4L3W2 (ODO1_EXISA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:EAT1b_2538
OrganismExiguobacterium sp. (strain ATCC BAA-1283 / AT1b) [Complete proteome] [HAMAP]
Taxonomic identifier360911 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length951 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 – 9519512-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169
PRO_1000213735

Sequences

Sequence LengthMass (Da)Tools
C4L3W2 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: BB172AC8134ADA9C

FASTA951106,924
        10         20         30         40         50         60 
MGESSNVHEK SQAFYGPNLG YIIELYEQYL EDPSSVDEET RRYFDEFGAP ETSTPTEVPV 

        70         80         90        100        110        120 
SGPSFDLEKV VSATRLINDI RAFGHKAADI YPLKDHPREQ ELFELSRYDL TEEDLKQIPA 

       130        140        150        160        170        180 
RLLSDDAPKP NASALELFRH LLDVYTGTVA IELRHLDDME EKKWIRRQVE QGALQQTFSK 

       190        200        210        220        230        240 
EEKIELFKRL AETELFESFL HKTYVGQKRF SIEGLDAMVP LLDAMVGGLI SSGSEHINIG 

       250        260        270        280        290        300 
MAHRGRLNVL AHVLGKPYEM IFAEFQHAPN KELIPSEGSI GINFGWSGDV KYHLGLDRKV 

       310        320        330        340        350        360 
VEQQKEVRLN LANNPSHLEF VGSVVEGYTR AAQDDRSEKG SAVQHDDLAA SILIHGDAAF 

       370        380        390        400        410        420 
PGQGIVAETL NMTNLTGYRT GGTVHVIANN TIGFTTDPND SRSTRYASDI AKGYEIPVFH 

       430        440        450        460        470        480 
VNADDPEACV AVAKLISEYR AKFHKDILVD LIGYRRYGHN EMDEPMNTNP VLYKAIKGHQ 

       490        500        510        520        530        540 
SVRHVYAARL EEEGVMTKDE KAQIEQKIEE ALKAARDLVP SEEEDADIVL PDAVHKGFPK 

       550        560        570        580        590        600 
VDTSVEREFL TQLNEELLNW PEGFGVFHKL QKVLDRRRDA FSEGGKIDWG HAETLAFASI 

       610        620        630        640        650        660 
LSDGTPVRLS GQDSERGTFA QRNIMLNDVE SGKKFSPLHE LSTAKASFSV YNSPLSEGSV 

       670        680        690        700        710        720 
LGFEYGYNVF AQDTLVLWEA QYGDFANSAQ VMFDQFISAG RAKWGQKSGL VMLLPHGYEG 

       730        740        750        760        770        780 
QGPEHSSARM ERYLTLAGEK NWTVANLSSA AQYFHILRRQ AEMLGKEEIR PMIIMTPKSL 

       790        800        810        820        830        840 
LRHPLATSPV EAFTEESFKP IVEQPGLGEN TEKVERLVFC TGKMAIDLAE AVGKSEESLD 

       850        860        870        880        890        900 
FLHIVRVEEI YPFPVREIRD VISRYPNARE IVWVQEEPKN MGAWTYIEPR LEAVTTNRLD 

       910        920        930        940        950 
VRYIGRRRRS SPAEGNPTAH KQEQARIIRE ALSRDVVSSG AGTSTYQKDR K 

« Hide

References

[1]"Complete sequence of Exiguobacterium sp. AT1b."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G. expand/collapse author list , Ramaley R.F., Rodrigues D.F., Vishnivetskaya T.A., Kathariou S., Tiedje J.M., Richardson P.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1283 / AT1b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001615 Genomic DNA. Translation: ACQ71457.1.
RefSeqYP_002886902.1. NC_012673.1.

3D structure databases

ProteinModelPortalC4L3W2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360911.EAT1b_2538.

Proteomic databases

PRIDEC4L3W2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ71457; ACQ71457; EAT1b_2538.
GeneID7870977.
KEGGeat:EAT1b_2538.
PATRIC21880348. VBIExiSp39724_2521.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycESP360911:GI4R-2634-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_EXISA
AccessionPrimary (citable) accession number: C4L3W2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: February 19, 2014
This is version 36 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