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Q5XI78 (ODO1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. 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, mitochondrial

EC=1.2.4.2
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E1
Short name=OGDC-E1
Alpha-ketoglutarate dehydrogenase
Gene names
Name:Ogdh
Synonyms:Ogdhl
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1023 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Catalytic activity

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate.

Enzyme regulation

Calcium ions and ADP stimulate, whereas ATP and NADH reduce catalytic activity By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandCalcium
Metal-binding
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from direct assay PubMed 3571202PubMed 9712727. Source: RGD

NADH metabolic process

Inferred from direct assay PubMed 9712727. Source: RGD

cerebellar cortex development

Inferred from electronic annotation. Source: Ensembl

generation of precursor metabolites and energy

Inferred from sequence or structural similarity. Source: UniProtKB

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

hippocampus development

Inferred from electronic annotation. Source: Ensembl

olfactory bulb mitral cell layer development

Inferred from electronic annotation. Source: Ensembl

pyramidal neuron development

Inferred from electronic annotation. Source: Ensembl

striatum development

Inferred from electronic annotation. Source: Ensembl

succinyl-CoA metabolic process

Inferred from direct assay PubMed 9712727. Source: RGD

tangential migration from the subventricular zone to the olfactory bulb

Inferred from electronic annotation. Source: Ensembl

thalamus development

Inferred from electronic annotation. Source: Ensembl

tricarboxylic acid cycle

Inferred from direct assay PubMed 9712727. Source: RGD

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 3571202PubMed 9712727PubMed 9811814. Source: RGD

oxoglutarate dehydrogenase complex

Inferred from direct assay PubMed 3571202. Source: RGD

   Molecular_functionchaperone binding

Inferred from physical interaction PubMed 9811814. Source: RGD

heat shock protein binding

Inferred from physical interaction PubMed 9811814. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxoglutarate dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: Ensembl

oxoglutarate dehydrogenase (succinyl-transferring) activity

Inferred from sequence or structural similarity. Source: UniProtKB

thiamine pyrophosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion By similarity
Chain41 – 10239832-oxoglutarate dehydrogenase, mitochondrial
PRO_0000271367

Regions

Calcium binding154 – 1585 By similarity

Sites

Metal binding1541Calcium By similarity

Amino acid modifications

Modified residue741N6-succinyllysine By similarity
Modified residue4011N6-acetyllysine By similarity
Modified residue5641N6-succinyllysine By similarity
Modified residue9701N6-acetyllysine By similarity
Cross-link534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5XI78 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: B258886383FBD98C

FASTA1,023116,296
        10         20         30         40         50         60 
MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE 

        70         80         90        100        110        120 
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV 

       130        140        150        160        170        180 
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES 

       190        200        210        220        230        240 
DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET 

       250        260        270        280        290        300 
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN 

       310        320        330        340        350        360 
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR 

       370        380        390        400        410        420 
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV 

       430        440        450        460        470        480 
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP 

       490        500        510        520        530        540 
EAVMYVCKVA AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY 

       550        560        570        580        590        600 
AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR 

       610        620        630        640        650        660 
SMTCPSTGLE EDILTHIGNV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA 

       670        680        690        700        710        720 
FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL 

       730        740        750        760        770        780 
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP 

       790        800        810        820        830        840 
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP NLQEENFDIS QLYDCNWIVV NCSTPGNFFH 

       850        860        870        880        890        900 
VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPEDGP AAQNPDKVKR 

       910        920        930        940        950        960 
LLFCTGKVYY DLTRERKARD MAEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH 

       970        980        990       1000       1010       1020 
KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK 


KFS 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[2]Lubec G., Afjehi-Sadat L.
Submitted (DEC-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 82-101; 123-135; 172-184 AND 583-600, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC083811 mRNA. Translation: AAH83811.1.
RefSeqNP_001017461.1. NM_001017461.1.
XP_006251508.1. XM_006251446.1.
XP_006251509.1. XM_006251447.1.
UniGeneRn.45991.

3D structure databases

ProteinModelPortalQ5XI78.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000008375.

2D gel databases

World-2DPAGE0004:Q5XI78.

Proteomic databases

PaxDbQ5XI78.
PRIDEQ5XI78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000057199; ENSRNOP00000054026; ENSRNOG00000005130.
GeneID360975.
KEGGrno:360975.

Organism-specific databases

CTD4967.
RGD1561359. Ogdh.

Phylogenomic databases

eggNOGCOG0567.
GeneTreeENSGT00530000063092.
HOGENOMHOG000259586.
HOVERGENHBG001892.
KOK00164.
OMAMLSGTHF.
OrthoDBEOG7FXZXH.
PhylomeDBQ5XI78.

Enzyme and pathway databases

SABIO-RKQ5XI78.

Gene expression databases

GenevestigatorQ5XI78.

Family and domain databases

Gene3D3.40.50.970. 2 hits.
InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
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]
SUPFAMSSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Other

NextBio674779.
PROQ5XI78.

Entry information

Entry nameODO1_RAT
AccessionPrimary (citable) accession number: Q5XI78
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 23, 2004
Last modified: July 9, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families