Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

Ogdh

Organism
Rattus norvegicus (Rat)
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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi154CalciumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi154 – 158By similarity5

GO - Molecular functioni

  • chaperone binding Source: RGD
  • heat shock protein binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • oxoglutarate dehydrogenase (NAD+) activity Source: RGD
  • oxoglutarate dehydrogenase (succinyl-transferring) activity Source: RGD
  • thiamine pyrophosphate binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandCalcium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiR-RNO-389661 Glyoxylate metabolism and glycine degradation
R-RNO-71064 Lysine catabolism
R-RNO-71403 Citric acid cycle (TCA cycle)
SABIO-RKiQ5XI78

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate dehydrogenase, mitochondrial (EC:1.2.4.2By similarity)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E1
Short name:
OGDC-E1
Alpha-ketoglutarate dehydrogenase
Gene namesi
Name:Ogdh
Synonyms:Ogdhl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi1561359 Ogdh

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
Transit peptidei1 – 40MitochondrionSequence analysisAdd BLAST40
ChainiPRO_000027136741 – 10232-oxoglutarate dehydrogenase, mitochondrialAdd BLAST983

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74N6-succinyllysineBy similarity1
Modified residuei100PhosphoserineBy similarity1
Modified residuei401N6-acetyllysineBy similarity1
Cross-linki534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei564N6-succinyllysineBy similarity1
Modified residuei970N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ5XI78
PRIDEiQ5XI78

2D gel databases

World-2DPAGEi0004:Q5XI78

PTM databases

iPTMnetiQ5XI78
PhosphoSitePlusiQ5XI78

Expressioni

Gene expression databases

BgeeiENSRNOG00000005130

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

GO - Molecular functioni

  • chaperone binding Source: RGD
  • heat shock protein binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000054026

Structurei

3D structure databases

ProteinModelPortaliQ5XI78
SMRiQ5XI78
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0450 Eukaryota
COG0567 LUCA
GeneTreeiENSGT00530000063092
HOGENOMiHOG000259586
HOVERGENiHBG001892
InParanoidiQ5XI78
KOiK00164
OMAiIDMVCYR
OrthoDBiEOG091G025G
PhylomeDBiQ5XI78

Family and domain databases

InterProiView protein in InterPro
IPR032106 2-oxogl_dehyd_N
IPR011603 2oxoglutarate_DH_E1
IPR001017 DH_E1
IPR031717 KGD_C
IPR029061 THDP-binding
IPR005475 Transketolase-like_Pyr-bd
PANTHERiPTHR23152 PTHR23152, 1 hit
PfamiView protein in Pfam
PF16078 2-oxogl_dehyd_N, 1 hit
PF00676 E1_dh, 1 hit
PF16870 OxoGdeHyase_C, 1 hit
PF02779 Transket_pyr, 1 hit
PIRSFiPIRSF000157 Oxoglu_dh_E1, 1 hit
SMARTiView protein in SMART
SM00861 Transket_pyr, 1 hit
SUPFAMiSSF52518 SSF52518, 2 hits
TIGRFAMsiTIGR00239 2oxo_dh_E1, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5XI78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL
60 70 80 90 100
SGTSSNYVEE MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS
110 120 130 140 150
RSSLATMAHA QSLVEAQPNV DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL
160 170 180 190 200
GILDADLDSS VPADIISSTD KLGFYGLHES DLDKVFHLPT TTFIGGQEPA
210 220 230 240 250
LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET PGIMQFTNEE
260 270 280 290 300
KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN
310 320 330 340 350
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH
360 370 380 390 400
LGMYHRRINR VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG
410 420 430 440 450
KKVMSILLHG DAAFAGQGIV YETFHLSDLP SYTTHGTVHV VVNNQIGFTT
460 470 480 490 500
DPRMARSSPY PTDVARVVNA PIFHVNSDDP EAVMYVCKVA AEWRNTFHKD
510 520 530 540 550
VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY AELLVSQGVV
560 570 580 590 600
NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR
610 620 630 640 650
SMTCPSTGLE EDILTHIGNV ASSVPVENFT IHGGLSRILK TRRELVTNRT
660 670 680 690 700
VDWALAEYMA FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC
710 720 730 740 750
IPMNHLWPNQ APYTVCNSSL SEYGVLGFEL GFAMASPNAL VLWEAQFGDF
760 770 780 790 800
NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP HGMEGMGPEH SSARPERFLQ
810 820 830 840 850
MCNDDPDVLP NLQEENFDIS QLYDCNWIVV NCSTPGNFFH VLRRQILLPF
860 870 880 890 900
RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPEDGP AAQNPDKVKR
910 920 930 940 950
LLFCTGKVYY DLTRERKARD MAEEVAITRI EQLSPFPFDL LLKEAQKYPN
960 970 980 990 1000
AELAWCQEEH KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK
1010 1020
THLTELQRFL DTAFDLDAFK KFS
Length:1,023
Mass (Da):116,296
Last modified:November 23, 2004 - v1
Checksum:iB258886383FBD98C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083811 mRNA Translation: AAH83811.1
RefSeqiNP_001017461.1, NM_001017461.1
XP_006251508.1, XM_006251446.3
XP_006251509.1, XM_006251447.2
XP_017460322.1, XM_017604833.1
XP_017460323.1, XM_017604834.1
UniGeneiRn.45991

Genome annotation databases

EnsembliENSRNOT00000057199; ENSRNOP00000054026; ENSRNOG00000005130
ENSRNOT00000083394; ENSRNOP00000068674; ENSRNOG00000005130
GeneIDi103693780
360975
KEGGirno:103693780
rno:360975

Similar proteinsi

Entry informationi

Entry nameiODO1_RAT
AccessioniPrimary (citable) accession number: Q5XI78
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 23, 2004
Last modified: March 28, 2018
This is version 103 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, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health