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Q5XI78

- ODO1_RAT

UniProt

Q5XI78 - ODO1_RAT

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Protein
2-oxoglutarate dehydrogenase, mitochondrial
Gene
Ogdh, Ogdhl
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi154 – 1541Calcium By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi154 – 1585 By similarity

GO - Molecular functioni

  1. chaperone binding Source: RGD
  2. heat shock protein binding Source: RGD
  3. metal ion binding Source: UniProtKB-KW
  4. oxoglutarate dehydrogenase (NAD+) activity Source: Ensembl
  5. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB
  6. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: RGD
  2. NADH metabolic process Source: RGD
  3. cerebellar cortex development Source: Ensembl
  4. generation of precursor metabolites and energy Source: UniProtKB
  5. glycolytic process Source: UniProtKB-KW
  6. hippocampus development Source: Ensembl
  7. olfactory bulb mitral cell layer development Source: Ensembl
  8. pyramidal neuron development Source: Ensembl
  9. striatum development Source: Ensembl
  10. succinyl-CoA metabolic process Source: RGD
  11. tangential migration from the subventricular zone to the olfactory bulb Source: Ensembl
  12. thalamus development Source: Ensembl
  13. tricarboxylic acid cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Calcium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiREACT_216424. Citric acid cycle (TCA cycle).
REACT_220761. Lysine catabolism.
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
ProteomesiUP000002494: Chromosome 14

Organism-specific databases

RGDi1561359. Ogdh.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrial membrane Source: UniProtKB
  3. mitochondrion Source: RGD
  4. oxoglutarate dehydrogenase complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040Mitochondrion By similarity
Add
BLAST
Chaini41 – 10239832-oxoglutarate dehydrogenase, mitochondrial
PRO_0000271367Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-succinyllysine By similarity
Modified residuei401 – 4011N6-acetyllysine By similarity
Cross-linki534 – 534Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei564 – 5641N6-succinyllysine By similarity
Modified residuei970 – 9701N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ5XI78.
PRIDEiQ5XI78.

2D gel databases

World-2DPAGE0004:Q5XI78.

Expressioni

Gene expression databases

GenevestigatoriQ5XI78.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008375.

Structurei

3D structure databases

ProteinModelPortaliQ5XI78.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0567.
GeneTreeiENSGT00530000063092.
HOGENOMiHOG000259586.
HOVERGENiHBG001892.
KOiK00164.
OMAiMLSGTHF.
OrthoDBiEOG7FXZXH.
PhylomeDBiQ5XI78.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 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

MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL     50
SGTSSNYVEE MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS 100
RSSLATMAHA QSLVEAQPNV DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL 150
GILDADLDSS VPADIISSTD KLGFYGLHES DLDKVFHLPT TTFIGGQEPA 200
LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET PGIMQFTNEE 250
KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN 300
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH 350
LGMYHRRINR VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG 400
KKVMSILLHG DAAFAGQGIV YETFHLSDLP SYTTHGTVHV VVNNQIGFTT 450
DPRMARSSPY PTDVARVVNA PIFHVNSDDP EAVMYVCKVA AEWRNTFHKD 500
VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY AELLVSQGVV 550
NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR 600
SMTCPSTGLE EDILTHIGNV ASSVPVENFT IHGGLSRILK TRRELVTNRT 650
VDWALAEYMA FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC 700
IPMNHLWPNQ APYTVCNSSL SEYGVLGFEL GFAMASPNAL VLWEAQFGDF 750
NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP HGMEGMGPEH SSARPERFLQ 800
MCNDDPDVLP NLQEENFDIS QLYDCNWIVV NCSTPGNFFH VLRRQILLPF 850
RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPEDGP AAQNPDKVKR 900
LLFCTGKVYY DLTRERKARD MAEEVAITRI EQLSPFPFDL LLKEAQKYPN 950
AELAWCQEEH KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK 1000
THLTELQRFL DTAFDLDAFK KFS 1023
Length:1,023
Mass (Da):116,296
Last modified:November 23, 2004 - v1
Checksum:iB258886383FBD98C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC083811 mRNA. Translation: AAH83811.1.
RefSeqiNP_001017461.1. NM_001017461.1.
XP_006251508.1. XM_006251446.1.
XP_006251509.1. XM_006251447.1.
UniGeneiRn.45991.

Genome annotation databases

EnsembliENSRNOT00000057199; ENSRNOP00000054026; ENSRNOG00000005130.
GeneIDi360975.
KEGGirno:360975.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC083811 mRNA. Translation: AAH83811.1 .
RefSeqi NP_001017461.1. NM_001017461.1.
XP_006251508.1. XM_006251446.1.
XP_006251509.1. XM_006251447.1.
UniGenei Rn.45991.

3D structure databases

ProteinModelPortali Q5XI78.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000008375.

2D gel databases

World-2DPAGE 0004:Q5XI78.

Proteomic databases

PaxDbi Q5XI78.
PRIDEi Q5XI78.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000057199 ; ENSRNOP00000054026 ; ENSRNOG00000005130 .
GeneIDi 360975.
KEGGi rno:360975.

Organism-specific databases

CTDi 4967.
RGDi 1561359. Ogdh.

Phylogenomic databases

eggNOGi COG0567.
GeneTreei ENSGT00530000063092.
HOGENOMi HOG000259586.
HOVERGENi HBG001892.
KOi K00164.
OMAi MLSGTHF.
OrthoDBi EOG7FXZXH.
PhylomeDBi Q5XI78.

Enzyme and pathway databases

Reactomei REACT_216424. Citric acid cycle (TCA cycle).
REACT_220761. Lysine catabolism.
SABIO-RK Q5XI78.

Miscellaneous databases

NextBioi 674779.
PROi Q5XI78.

Gene expression databases

Genevestigatori Q5XI78.

Family and domain databases

Gene3Di 3.40.50.970. 2 hits.
InterProi IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

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: September 3, 2014
This is version 77 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

External Data

Dasty 3

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