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Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

Ogdh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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.

Cofactori

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Calcium, 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-RKQ5XI78.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ogdh
Synonyms:Ogdhl
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi1561359. Ogdh.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrial membrane Source: UniProtKB
  • mitochondrion Source: RGD
  • oxoglutarate dehydrogenase complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 40MitochondrionBy similarityAdd 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-2DPAGE0004:Q5XI78.

PTM databases

iPTMnetiQ5XI78.
PhosphoSitePlusiQ5XI78.

Expressioni

Gene expression databases

BgeeiENSRNOG00000005130.

Interactioni

GO - Molecular functioni

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000054026.

Structurei

3D structure databases

ProteinModelPortaliQ5XI78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0450. Eukaryota.
COG0567. LUCA.
GeneTreeiENSGT00530000063092.
HOGENOMiHOG000259586.
HOVERGENiHBG001892.
InParanoidiQ5XI78.
KOiK00164.
OMAiSHYNFTE.
OrthoDBiEOG091G025G.
PhylomeDBiQ5XI78.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR032106. 2-oxogl_dehyd_N.
IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR031717. KGD_C.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF16078. 2-oxogl_dehyd_N. 1 hit.
PF00676. E1_dh. 1 hit.
PF16870. OxoGdeHyase_C. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
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:360975.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ5XI78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000054026.

PTM databases

iPTMnetiQ5XI78.
PhosphoSitePlusiQ5XI78.

2D gel databases

World-2DPAGE0004:Q5XI78.

Proteomic databases

PaxDbiQ5XI78.
PRIDEiQ5XI78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000057199; ENSRNOP00000054026; ENSRNOG00000005130.
ENSRNOT00000083394; ENSRNOP00000068674; ENSRNOG00000005130.
GeneIDi103693780.
360975.
KEGGirno:360975.

Organism-specific databases

CTDi4967.
RGDi1561359. Ogdh.

Phylogenomic databases

eggNOGiKOG0450. Eukaryota.
COG0567. LUCA.
GeneTreeiENSGT00530000063092.
HOGENOMiHOG000259586.
HOVERGENiHBG001892.
InParanoidiQ5XI78.
KOiK00164.
OMAiSHYNFTE.
OrthoDBiEOG091G025G.
PhylomeDBiQ5XI78.

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-RKQ5XI78.

Miscellaneous databases

PROiQ5XI78.

Gene expression databases

BgeeiENSRNOG00000005130.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR032106. 2-oxogl_dehyd_N.
IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR031717. KGD_C.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF16078. 2-oxogl_dehyd_N. 1 hit.
PF00676. E1_dh. 1 hit.
PF16870. OxoGdeHyase_C. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiODO1_RAT
AccessioniPrimary (citable) accession number: Q5XI78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 23, 2004
Last modified: November 30, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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.