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Q5XI78

- ODO1_RAT

UniProt

Q5XI78 - ODO1_RAT

Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

Ogdh

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    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

    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 – 1541CalciumBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi154 – 1585By 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. cerebellar cortex development Source: Ensembl
    3. generation of precursor metabolites and energy Source: UniProtKB
    4. glycolytic process Source: UniProtKB-KW
    5. hippocampus development Source: Ensembl
    6. NADH metabolic process Source: RGD
    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

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4040MitochondrionBy similarityAdd
    BLAST
    Chaini41 – 10239832-oxoglutarate dehydrogenase, mitochondrialPRO_0000271367Add
    BLAST

    Amino acid modifications

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

    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

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    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

    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: October 1, 2014
    This is version 78 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