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P53395

- ODB2_MOUSE

UniProt

P53395 - ODB2_MOUSE

Protein

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

Gene

Dbt

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.

    Catalytic activityi

    2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei452 – 4521Sequence Analysis
    Active sitei456 – 4561Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC:2.3.1.168)
    Alternative name(s):
    Branched-chain alpha-keto acid dehydrogenase complex component E2
    Short name:
    BCKAD-E2
    Short name:
    BCKADE2
    Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
    Dihydrolipoamide branched chain transacylase
    Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
    Gene namesi
    Name:Dbt
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:105386. Dbt.

    Subcellular locationi

    GO - Cellular componenti

    1. microtubule cytoskeleton Source: Ensembl
    2. mitochondrial nucleoid Source: Ensembl
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6161MitochondrionSequence AnalysisAdd
    BLAST
    Chaini62 – 482421Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrialPRO_0000020490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051N6-lipoyllysineBy similarity
    Modified residuei133 – 1331N6-succinyllysine1 Publication
    Modified residuei196 – 1961N6-acetyllysine; alternate1 Publication
    Modified residuei196 – 1961N6-succinyllysine; alternate1 Publication
    Modified residuei202 – 2021N6-acetyllysine1 Publication
    Modified residuei243 – 2431N6-acetyllysine1 Publication
    Modified residuei250 – 2501N6-acetyllysine1 Publication
    Modified residuei261 – 2611N6-succinyllysine1 Publication
    Modified residuei289 – 2891N6-acetyllysine; alternate1 Publication
    Modified residuei289 – 2891N6-succinyllysine; alternate1 Publication
    Modified residuei295 – 2951N6-acetyllysine1 Publication
    Modified residuei304 – 3041N6-acetyllysine1 Publication
    Modified residuei435 – 4351N6-acetyllysine1 Publication
    Modified residuei440 – 4401N6-acetyllysine; alternate1 Publication
    Modified residuei440 – 4401N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP53395.
    PaxDbiP53395.
    PRIDEiP53395.

    PTM databases

    PhosphoSiteiP53395.

    Expressioni

    Gene expression databases

    BgeeiP53395.
    CleanExiMM_DBT.
    GenevestigatoriP53395.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Protein-protein interaction databases

    BioGridi199061. 4 interactions.
    IntActiP53395. 5 interactions.
    MINTiMINT-1860345.
    STRINGi10090.ENSMUSP00000000349.

    Structurei

    3D structure databases

    ProteinModelPortaliP53395.
    SMRiP53395. Positions 62-147, 165-213, 249-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 13874Lipoyl-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.
    GeneTreeiENSGT00740000115255.
    HOGENOMiHOG000281564.
    HOVERGENiHBG104085.
    InParanoidiQ3TMF5.
    KOiK09699.
    OMAiEPLKGFH.
    OrthoDBiEOG7GFB4W.
    TreeFamiTF314182.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR015761. BCKDC_E2.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PANTHERiPTHR23151:SF46. PTHR23151:SF46. 1 hit.
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 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.

    P53395-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAARVLRTW SQNAVRLTCV RYFQTFNSAR VLKPKCVCSV GYPLFKYSQP    50
    RHSLRTAAVL QGQVVQFKLS DIGEGIREVT IKEWYVKEGD TVSQFDSICE 100
    VQSDKASVTI TSRYDGVIKR LYYNLDDIAY VGKPLIDIET EALKDSEEDV 150
    VETPAVSHDE HTHQEIKGQK TLATPAVRRL AMENNIKLSE VVGSGKDGRI 200
    LKEDILSFLE KQTGAILPPS PKSEITPPPP QPKDRTFPTP IAKPPVFTGK 250
    DRTEPVTGFQ KAMVKTMSAA LKIPHFGYCD EIDLTQLVKL REELKPVALA 300
    RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT 350
    ELGLIVPNVK NVQVRSVFEI AMELNRLQKL GSSGQLGTTD LTGGTFTLSN 400
    IGSIGGTYAK PVILPPEVAI GALGAIKALP RFDQKGDVYK AQIMNVSWSA 450
    DHRVIDGATM SRFSNLWKSY LENPAFMLLD LK 482
    Length:482
    Mass (Da):53,247
    Last modified:July 27, 2011 - v2
    Checksum:i79E440D1B4B9B948
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti369 – 3713EIA → GIG in AAC37681. (PubMed:8605244)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42996 mRNA. Translation: AAC37681.1.
    AK165959 mRNA. Translation: BAE38487.1.
    CH466532 Genomic DNA. Translation: EDL12381.1.
    CCDSiCCDS17787.1.
    PIRiS65760.
    RefSeqiNP_034152.2. NM_010022.3.
    UniGeneiMm.3636.

    Genome annotation databases

    EnsembliENSMUST00000000349; ENSMUSP00000000349; ENSMUSG00000000340.
    GeneIDi13171.
    KEGGimmu:13171.
    UCSCiuc008rcg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42996 mRNA. Translation: AAC37681.1 .
    AK165959 mRNA. Translation: BAE38487.1 .
    CH466532 Genomic DNA. Translation: EDL12381.1 .
    CCDSi CCDS17787.1.
    PIRi S65760.
    RefSeqi NP_034152.2. NM_010022.3.
    UniGenei Mm.3636.

    3D structure databases

    ProteinModelPortali P53395.
    SMRi P53395. Positions 62-147, 165-213, 249-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199061. 4 interactions.
    IntActi P53395. 5 interactions.
    MINTi MINT-1860345.
    STRINGi 10090.ENSMUSP00000000349.

    PTM databases

    PhosphoSitei P53395.

    Proteomic databases

    MaxQBi P53395.
    PaxDbi P53395.
    PRIDEi P53395.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000349 ; ENSMUSP00000000349 ; ENSMUSG00000000340 .
    GeneIDi 13171.
    KEGGi mmu:13171.
    UCSCi uc008rcg.2. mouse.

    Organism-specific databases

    CTDi 1629.
    MGIi MGI:105386. Dbt.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115255.
    HOGENOMi HOG000281564.
    HOVERGENi HBG104085.
    InParanoidi Q3TMF5.
    KOi K09699.
    OMAi EPLKGFH.
    OrthoDBi EOG7GFB4W.
    TreeFami TF314182.

    Miscellaneous databases

    NextBioi 283268.
    PROi P53395.
    SOURCEi Search...

    Gene expression databases

    Bgeei P53395.
    CleanExi MM_DBT.
    Genevestigatori P53395.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR015761. BCKDC_E2.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    PANTHERi PTHR23151:SF46. PTHR23151:SF46. 1 hit.
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the murine branched chain alpha-ketoacid dehydrogenase E2 subunit: presence of 3' B1 repeat elements."
      Costeas P.A., Tonelli L.A., Chinsky J.M.
      Biochim. Biophys. Acta 1305:25-28(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-196; LYS-261; LYS-289 AND LYS-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196; LYS-202; LYS-243; LYS-250; LYS-289; LYS-295; LYS-304; LYS-435 AND LYS-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiODB2_MOUSE
    AccessioniPrimary (citable) accession number: P53395
    Secondary accession number(s): Q3TMF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 117 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, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3