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P11179

- ODO2_BOVIN

UniProt

P11179 - ODO2_BOVIN

Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

DLST

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      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 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

    Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei426 – 4261Sequence Analysis
    Active sitei430 – 4301Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    2. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.61)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E2
    Short name:
    OGDC-E2
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
    E2K
    Gene namesi
    Name:DLST
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. oxoglutarate dehydrogenase complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6868MitochondrionBy similarityAdd
    BLAST
    Chaini69 – 455387Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000162252Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei111 – 1111N6-lipoyllysine1 Publication
    Modified residuei155 – 1551N6-acetyllysineBy similarity
    Modified residuei269 – 2691N6-acetyllysineBy similarity
    Modified residuei274 – 2741N6-acetyllysineBy similarity
    Modified residuei275 – 2751N6-acetyllysineBy similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity
    Modified residuei309 – 3091N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP11179.
    PRIDEiP11179.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Protein-protein interaction databases

    IntActiP11179. 1 interaction.
    STRINGi9913.ENSBTAP00000052502.

    Structurei

    3D structure databases

    ProteinModelPortaliP11179.
    SMRiP11179. Positions 226-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 14473Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281563.
    HOVERGENiHBG000268.
    KOiK00658.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    TIGRFAMsiTIGR01347. sucB. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P11179-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSRSRCASR AFSRSLSAFQ KGNCPLVRRS LPGISLCQGP GYPDSRKTVI    50
    NSSNIFSVRF FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE 100
    DEVVCEIETD KTSVQVPSPA NGVIEALLVP DGGKVEGGTP LFTLRKTGAA 150
    PAKAKPAAAP AAAAPKAEPT VSAVPPPPAA PIPTQMPPVP SPSQPLTSKP 200
    VSAVKPTAAP PRAEAGAGVG LRSEHREKMN RMRQRIAQRL KEAQNTCAML 250
    TTFNEIDMSN IQEMRARHKD AFLKKHNLKL GFMSAFVKAS AFALQEQPVV 300
    NAVIDDATKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS 350
    ELGEKARKNE LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA 400
    IVDRPVVIGG KVEVRPMMYV ALTYDHRLID GREAVTFLRK IKAAVEDPRV 450
    LLLDL 455
    Length:455
    Mass (Da):48,973
    Last modified:October 17, 2006 - v2
    Checksum:iDB2124A4D06C389B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT026207 mRNA. Translation: ABG67046.1.
    PIRiS00123.
    RefSeqiNP_001068750.1. NM_001075282.1.
    UniGeneiBt.41191.

    Genome annotation databases

    GeneIDi506888.
    KEGGibta:506888.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT026207 mRNA. Translation: ABG67046.1 .
    PIRi S00123.
    RefSeqi NP_001068750.1. NM_001075282.1.
    UniGenei Bt.41191.

    3D structure databases

    ProteinModelPortali P11179.
    SMRi P11179. Positions 226-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11179. 1 interaction.
    STRINGi 9913.ENSBTAP00000052502.

    Proteomic databases

    PaxDbi P11179.
    PRIDEi P11179.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 506888.
    KEGGi bta:506888.

    Organism-specific databases

    CTDi 1743.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281563.
    HOVERGENi HBG000268.
    KOi K00658.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .

    Miscellaneous databases

    NextBioi 20867785.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR011053. Single_hybrid_motif.
    IPR006255. SucB.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    TIGRFAMsi TIGR01347. sucB. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "Amino acid sequence surrounding the lipoic acid cofactor of bovine kidney 2-oxoglutarate dehydrogenase complex."
      Bradford A.P., Aitken A., Beg F., Cook K.G., Yeaman S.J.
      FEBS Lett. 222:211-214(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 107-122, LIPOYLATION AT LYS-111.
      Tissue: Kidney.

    Entry informationi

    Entry nameiODO2_BOVIN
    AccessioniPrimary (citable) accession number: P11179
    Secondary accession number(s): Q0V8L1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 102 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3