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Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

OGDH

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

Functioni

2-oxoglutarate dehydrogenase (E1) component of the 2-oxoglutarate dehydrogenase complex, which mediates the decarboxylation of alpha-ketoglutarate. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A.By similarity

Catalytic activityi

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

Cofactori

thiamine diphosphateBy similarity

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandThiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase, mitochondrialBy similarity (EC:1.2.4.2By similarity)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeMesocricetus
Proteomesi

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Nucleus

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

Interactioni

Subunit structurei

The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the The 2-oxoglutarate dehydrogenase complex associates with KAT2A.By similarity

Structurei

3D structure databases

SMRiP86231
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiView protein in InterPro
IPR011603 2oxoglutarate_DH_E1
PANTHERiPTHR23152 PTHR23152, 6 hits

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

Entry informationi

Entry nameiODO1_MESAU
AccessioniPrimary (citable) accession number: P86231
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: March 28, 2018
This is version 26 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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