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A8FE66 (ODO1_BACP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:BPUM_1862
OrganismBacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]
Taxonomic identifier315750 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length944 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 – 9449442-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169
PRO_1000065697

Sequences

Sequence LengthMass (Da)Tools
A8FE66 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 5CF1400B2F45876F

FASTA944106,822
        10         20         30         40         50         60 
MFQNDVKQPL SWEEFHGPNL GYVLELYDQY VQDPTSVDED LRGIFDELGA PPSEMKEEIG 

        70         80         90        100        110        120 
KKENSVVTSE QIQKIASVVK LAEDIRTYGH LNASVNPLRK EKELQELFPL KEYGLTEEDV 

       130        140        150        160        170        180 
KNIPISIISP DAPKHISNGI EAINHLRNTY KRTISFEFDH VHDFEERNWL SKSIESGELF 

       190        200        210        220        230        240 
KKKPADKLVS VFKRLTEVEQ FEQFLHKTFV GQKRFSIEGL DALVPVLDEI ISESVTQGTS 

       250        260        270        280        290        300 
NINIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPNKELVP SEGSIGISYG WTGDVKYHLG 

       310        320        330        340        350        360 
ADRQIKDEDT KSARVTLANN PSHLEFIDPI IEGSTRAAQE LRTQKGYPAQ DVEKALAILI 

       370        380        390        400        410        420 
HGDAAFPGEG IVAETLNLSQ LVGYQVGGTI HIIANNMIGF TTESNESRST KYASDLAKGF 

       430        440        450        460        470        480 
EIPIVHVNAD DPEACLAAVQ LAVEYRKRFK KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD 

       490        500        510        520        530        540 
AVRKHKTVKN IFADKLVSEG LLTKEQREEI EQAVATRIEE AYQKVPSKKE HTIQEIELPE 

       550        560        570        580        590        600 
PVSNGFPAVD TSVEFDVLRK LNEELISWPD DFQVFGKLKR ILEKRAKVFT DDRKVEWSLG 

       610        620        630        640        650        660 
EALAFASILK DGTPIRMTGQ DSERGTFAQR NLVLHDSQTG NEFIALHELS DANASFTVHN 

       670        680        690        700        710        720 
SPLSEGSVIG FEYGYNVYSP ETLVIWEAQF GDFANAAQVY FDQFISAGRA KWGQKSGLVM 

       730        740        750        760        770        780 
LLPHGYEGQG PEHSSGRTER FLQSAAENNW TVANLTSAAQ YFHILRRQAK MLLREEIRPL 

       790        800        810        820        830        840 
VIMTPKSLLR NPNSLSEVQE LTDGQFQPVL EQPGLVHDHE KVSRLVLSSG KVSIDISDRF 

       850        860        870        880        890        900 
TQMEEPKDWL HIARVEQLYP FPAKDIKAIL SKLTNLEEIV WTQEEPQNMG AWGYIEPYLR 

       910        920        930        940 
EIAPEKVKVR YIGRRRRSST AEGDPTVHKK EQERIVSDSL TRKN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000813 Genomic DNA. Translation: ABV62533.1.
RefSeqYP_001487093.1. NC_009848.1.

3D structure databases

ProteinModelPortalA8FE66.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315750.BPUM_1862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV62533; ABV62533; BPUM_1862.
GeneID5621130.
KEGGbpu:BPUM_1862.
PATRIC18967612. VBIBacPum16546_1902.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBPUM315750:GH6N-1918-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_BACP2
AccessionPrimary (citable) accession number: A8FE66
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 48 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