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Q65IH4 (ODO1_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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:BLi02260, BL01452
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [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_0000162167

Sequences

Sequence LengthMass (Da)Tools
Q65IH4 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 9E63C701C8847E39

FASTA944106,671
        10         20         30         40         50         60 
MFQNSMKQRM TWEEFHGPNL GYVLELYDQY VKDPESLDAD LKEMFDELGA PPGDIRAASQ 

        70         80         90        100        110        120 
KNEEADFTAG SIQKIASAVK LAEDIRTYGH LNASVNPLRK TQEKQELFPL AEYGLTEQDV 

       130        140        150        160        170        180 
KKIPASVICK DAPKEVTNGL EAIQYLRNTY KKSISFEFDH VHIFEERNWL MKKIESGELF 

       190        200        210        220        230        240 
TPKSKEKLVE VLRRLTEVES LEQFLHKTFV GQKRFSIEGL DALVPMLDDI IAKSVSAGTT 

       250        260        270        280        290        300 
NVNIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSTGINYG WTGDVKYHLG 

       310        320        330        340        350        360 
ANRQIQDEHT KTARIALANN PSHLEFIDPI VEGSTRAAQE TRTESGYPVQ DVKKSMAILI 

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

       430        440        450        460        470        480 
EIPIVHVNAD DPEACLSAVQ LAVEYRMTFN KDFLIDLIGY RRFGHNEMDE PSATQPMLYD 

       490        500        510        520        530        540 
AVRKHPTVKN IFAEKLIHKG IVDKETVGKI KDAVQKRLEE AYRKVPAKKE DMTHEIVLPE 

       550        560        570        580        590        600 
PVSNGFPDVD TSVDFETLRK INQELVSWPE NFNVFDKLKR ILERRAKAFE DDRKVDWSLA 

       610        620        630        640        650        660 
EAMAFASILK DGTPLRLTGQ DSERGTFAHR NLVLHDSKTG DEFIALHHLA DTKASFAVHN 

       670        680        690        700        710        720 
SPLSEGSVLG FEYGYNVSSP ETMVIWEAQF GDFANAAQVY FDQFISAGRA KWGQKSGLVV 

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

       790        800        810        820        830        840 
IIMTPKSLLR NPNTVSEVQE LSNSSFKPVY EMSGLSHQYD KVTRLVLSSG KVSIDISDHF 

       850        860        870        880        890        900 
NKMEGEKDWL HIARVEELYP FPAKHIKAIF SKLPNLEEIV WVQEEPQNMG AWNYIEPYLR 

       910        920        930        940 
EVAPKDVKVR YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU41140.1.
CP000002 Genomic DNA. Translation: AAU23783.1.
RefSeqYP_006713619.1. NC_006322.1.
YP_079421.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65IH4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL01452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU23783; AAU23783; BL01452.
AAU41140; AAU41140; BLi02260.
GeneID3028258.
3100388.
KEGGbld:BLi02260.
bli:BL01452.
PATRIC18950158. VBIBacLic203714_2281.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0567.
HOGENOMHOG000259588.
KOK00164.
OMANEGVANE.
OrthoDBEOG6V1M1F.
ProtClustDBPRK09404.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-2245-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_BACLD
AccessionPrimary (citable) accession number: Q65IH4
Secondary accession number(s): Q62TX6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 25, 2004
Last modified: February 19, 2014
This is version 66 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