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Q5RCB8

- ODO1_PONAB

UniProt

Q5RCB8 - ODO1_PONAB

Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

OGDH

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (21 Dec 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.By similarity

    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. metal ion binding Source: UniProtKB-KW
    2. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB
    3. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. generation of precursor metabolites and energy Source: UniProtKB
    2. glycolytic process Source: UniProtKB-KW
    3. tricarboxylic acid cycle Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Calcium, Metal-binding, Thiamine pyrophosphate

    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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrial membrane Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4040MitochondrionBy similarityAdd
    BLAST
    Chaini41 – 10239832-oxoglutarate dehydrogenase, mitochondrialPRO_0000020435Add
    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

    PRIDEiQ5RCB8.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RCB8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG001892.
    InParanoidiQ5RCB8.
    KOiK00164.

    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.

    Q5RCB8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL     50
    SGTSSNYVEE MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS 100
    RGSLAAVAHA QSLVEAQPNV DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL 150
    GILDADLDSS VPADIISSTD KLGFYGLDES DLDKVFHLPT TTFIGGQESA 200
    LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET PGIMQFTNEE 250
    KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN 300
    GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH 350
    LGMYHRRINR VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG 400
    KKVMSILLHG DAAFAGQGIV YETFHLSDLP SYTTHGTVHV VVNNQIGFTT 450
    DPRMARSSPY PTDVARVVNA PIFHVNSDDP EAVMYVCKVA AEWRSTFHKD 500
    VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY AELLVSQGVV 550
    NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR 600
    SMSCPSTGLT EDILTHIGNV ASSVPVENFT IHGGLSRILK TRGEMVKNRT 650
    VDWALAEYMA FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC 700
    IPMNHLWPNQ APYTVCNSSL SEYGVLGFEL GFAMASPNAL VLWEAQFGDF 750
    HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP HGMEGMGPEH SSARPERFLQ 800
    MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH VLRRQILLPF 850
    RKPLIIFTPK SLLRHPEARS SFDEMLPGTH FQRVIPEDGP AAQNPENVKR 900
    LLFCTGKVYY DLTRERKARD MVGQVAITRI EQLSPFPFDL LLKEVQKYPS 950
    AELAWCQEEH KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK 1000
    THLTELQRLL DTAFDLDIFK NFS 1023
    Length:1,023
    Mass (Da):115,922
    Last modified:December 21, 2004 - v1
    Checksum:iF432EE1D3502977C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858358 mRNA. Translation: CAH90589.1.
    RefSeqiNP_001125317.1. NM_001131845.1.

    Genome annotation databases

    GeneIDi100172216.
    KEGGipon:100172216.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR858358 mRNA. Translation: CAH90589.1 .
    RefSeqi NP_001125317.1. NM_001131845.1.

    3D structure databases

    ProteinModelPortali Q5RCB8.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5RCB8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100172216.
    KEGGi pon:100172216.

    Organism-specific databases

    CTDi 4967.

    Phylogenomic databases

    HOVERGENi HBG001892.
    InParanoidi Q5RCB8.
    KOi K00164.

    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 German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiODO1_PONAB
    AccessioniPrimary (citable) accession number: Q5RCB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 63 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3