Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8CUL8 (ODO1_OCEIH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:OB1089
OrganismOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]
Taxonomic identifier221109 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeOceanobacillus

Protein attributes

Sequence length953 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 – 9539532-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169
PRO_0000162175

Sequences

Sequence LengthMass (Da)Tools
Q8CUL8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 78AB32B7CFBE7A6E

FASTA953107,266
        10         20         30         40         50         60 
MAENAESAER FWGQFHGQNT GYLEQQFELY KEDPELVESS IRTIFDTHGA PSWLSSTENV 

        70         80         90        100        110        120 
KSVSNASDFD VTKLTSAIRL VEAIRRYGHT DADIYPVGGY KGDRSKMLDL STYNLKEQDL 

       130        140        150        160        170        180 
EKIPASWIWE KQAPGVATAL DVVNQLKKYY TGTITFEYDH VNNDEERKWL FDLIEEGNAR 

       190        200        210        220        230        240 
LDPSDDERKK ILQRLADVEG FEKFLHKTFV GQKRFSIEGL ESMVPMIDHI VQYSNQDSIE 

       250        260        270        280        290        300 
HVMMGMAHRG RLSVLANVLG KPYDKIFSEF NYTKEKELMP SEGSRAINYG WTGDVKYHYG 

       310        320        330        340        350        360 
AEKEVEFGNK GQTRITLAHN PSHLEFVNPV VEGFTRAAQD DRSEKGYPKQ VTNKAVSVLI 

       370        380        390        400        410        420 
HGDAAFIGEG VVAETLNLSG LPGYSTGGTL HIIANNLLGY TTDREDGRST RYASDLAKGF 

       430        440        450        460        470        480 
EIPVIRVNAD DPISCISAIK IAYEYRQKFQ KDFLIDLVGY RRYGHNEMDE PRTTQPSLYQ 

       490        500        510        520        530        540 
QIDDHPSVAS LFGKGMEEKG ILQEGGFEEV KSAVEKKLTD IYKGMTESEI GEPEAKLMPQ 

       550        560        570        580        590        600 
VLTNGLDQFT TAIDLATLKS INEELLERPE GFKGFKKTER ILQRRKDALE EGNKADWGTG 

       610        620        630        640        650        660 
EALAFASILK EGTPIRLTGQ DTERGTFAHR HIVLHDVETG EKYSPLHGLS DVEASFDVRN 

       670        680        690        700        710        720 
SPLSEAGVLG FEYGYSVQSP DTLVIWEAQF GDFANAGQVI FDQFISSARA KWGEKSNMVL 

       730        740        750        760        770        780 
LLPHGYEGQG PEHSSARLER FLQMAAENNW IVANVTSSAQ LFHILRRQAA MRDRDEARPL 

       790        800        810        820        830        840 
VLMTPKSSLI RHPRMGATAE EFTDGGFLAL RDQPGFEANR EKVTRLVVGS GKMMIDIEEA 

       850        860        870        880        890        900 
MDDSDETYDW LQIKRVEQIY PFPKKALEEE IKQLPNLKEI VWVQEEPKNM GAWNFVDDYL 

       910        920        930        940        950 
RELLNEDQKL KVISRPDRSA PAGGIPTVHK TAQNKIIKQA LNQSEGGKSS AGN 

« Hide

References

[1]"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000028 Genomic DNA. Translation: BAC13045.1.
RefSeqNP_692010.1. NC_004193.1.

3D structure databases

ProteinModelPortalQ8CUL8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING221109.OB1089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC13045; BAC13045; BAC13045.
GeneID1017056.
KEGGoih:OB1089.
PATRIC22793182. VBIOceIhe82024_1108.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0567.
HOGENOMHOG000259588.
KOK00164.
OMAHILRRQL.
OrthoDBEOG6V1M1F.
ProtClustDBPRK09404.

Enzyme and pathway databases

BioCycOIHE221109:GI2A-1165-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_OCEIH
AccessionPrimary (citable) accession number: Q8CUL8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 70 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