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Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

OGDH

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

thiamine diphosphateBy similarity

Enzyme regulationi

Catabolite repressed.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase, mitochondrialBy similarity (EC:1.2.4.2)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E1By similarity
Short name:
OGDC-E1By similarity
Alpha-ketoglutarate dehydrogenaseBy similarity
Gene namesi
Name:OGDHBy similarity
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

  • Mitochondrion matrix By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003947381 – ›1802-oxoglutarate dehydrogenase, mitochondrialAdd BLAST›180

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14N6-succinyllysineBy similarity1
Modified residuei40PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP86231.

Structurei

3D structure databases

ProteinModelPortaliP86231.
SMRiP86231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-ketoglutarate dehydrogenase family.Sequence analysis

Family and domain databases

InterProiIPR011603. 2oxoglutarate_DH_E1.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.

Sequencei

Sequence statusi: Fragments.

P86231-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFHLRTCAAK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RLGFYGLHES
60 70 80 90 100
DLDKSTRFEE FLQRGRLNVL ANVIRYHLGM YHRRSSPYPT DVARICEEAF
110 120 130 140 150
TRRQILLPFR KPLIVFTPKS LLRHPEARTS FDEMLPGTHF QRVYYDLTRA
160 170 180
KPVWYAGRKT HLTELQRFLD TAFDLDAFKK
Length:180
Mass (Da):21,097
Last modified:June 15, 2010 - v1
Checksum:i6C78EA048791E270
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-adjacent residuesi10 – 11Curated2
Non-adjacent residuesi41 – 42Curated2
Non-adjacent residuesi54 – 55Curated2
Non-adjacent residuesi64 – 65Curated2
Non-adjacent residuesi75 – 76Curated2
Non-adjacent residuesi84 – 85Curated2
Non-adjacent residuesi94 – 95Curated2
Non-adjacent residuesi102 – 103Curated2
Non-adjacent residuesi142 – 143Curated2
Non-adjacent residuesi149 – 150Curated2
Non-adjacent residuesi158 – 159Curated2
Non-terminal residuei1801

Cross-referencesi

3D structure databases

ProteinModelPortaliP86231.
SMRiP86231.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP86231.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR011603. 2oxoglutarate_DH_E1.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiODO1_MESAU
AccessioniPrimary (citable) accession number: P86231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: November 2, 2016
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.