Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P65634

- ODP2_MYCBO

UniProt

P65634 - ODP2_MYCBO

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

dlaT

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.By similarity

    Catalytic activityi

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 2 lipoyl cofactors covalently.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei523 – 5231By similarity
    Active sitei527 – 5271By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Glycolysis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)
    Alternative name(s):
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    Pyruvate dehydrogenase complex component E2
    Short name:
    PDH component E2
    Gene namesi
    Name:dlaT
    Synonyms:sucB
    Ordered Locus Names:Mb2238
    OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
    Taxonomic identifieri233413 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001419: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 553553Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162267Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-lipoyllysineSequence Analysis
    Modified residuei162 – 1621N6-lipoyllysineSequence Analysis

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry. Part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3).By similarity

    Protein-protein interaction databases

    STRINGi233413.Mb2238.

    Structurei

    3D structure databases

    ProteinModelPortaliP65634.
    SMRiP65634. Positions 3-76, 126-195, 322-544.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7676Lipoyl-binding 1Add
    BLAST
    Domaini122 – 19574Lipoyl-binding 2Add
    BLAST
    Domaini241 – 27838E3-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 E3-binding domain.Curated
    Contains 2 lipoyl-binding domains.Curated

    Keywords - Domaini

    Lipoyl, Repeat

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281564.
    KOiK00658.
    OMAiQEDETVE.

    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.
    IPR014276. 2-oxoglutarate_DH_E2.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsiTIGR02927. SucB_Actino. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P65634-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFSVQMPAL GESVTEGTVT RWLKQEGDTV ELDEPLVEVS TDKVDTEIPS    50
    PAAGVLTKII AQEDDTVEVG GELAVIGDAK DAGEAAAPAP EKVPAAQPES 100
    KPAPEPPPVQ PTSGAPAGGD AKPVLMPELG ESVTEGTVIR WLKKIGDSVQ 150
    VDEPLVEVST DKVDTEIPSP VAGVLVSISA DEDATVPVGG ELARIGVAAD 200
    IGAAPAPKPA PKPVPEPAPT PKAEPAPSPP AAQPAGAAEG APYVTPLVRK 250
    LASENNIDLA GVTGTGVGGR IRKQDVLAAA EQKKRAKAPA PAAQAAAAPA 300
    PKAPPAPAPA LAHLRGTTQK ASRIRQITAN KTRESLQATA QLTQTHEVDM 350
    TKIVGLRARA KAAFAEREGV NLTFLPFFAK AVIDALKIHP NINASYNEDT 400
    KEITYYDAEH LGFAVDTEQG LLSPVIHDAG DLSLAGLARA IADIAARARS 450
    GNLKPDELSG GTFTITNIGS QGALFDTPIL VPPQAAMLGT GAIVKRPRVV 500
    VDASGNESIG VRSVCYLPLT YDHRLIDGAD AGRFLTTIKH RLEEGAFEAD 550
    LGL 553
    Length:553
    Mass (Da):57,088
    Last modified:October 11, 2004 - v1
    Checksum:i54B6E70D23B804A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO43492.1.
    RefSeqiNP_855887.1. NC_002945.3.

    Genome annotation databases

    EnsemblBacteriaiCAD97091; CAD97091; Mb2238.
    GeneIDi1091362.
    KEGGimbo:Mb2238.
    PATRICi18006616. VBIMycBov88188_2454.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO43492.1 .
    RefSeqi NP_855887.1. NC_002945.3.

    3D structure databases

    ProteinModelPortali P65634.
    SMRi P65634. Positions 3-76, 126-195, 322-544.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 233413.Mb2238.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD97091 ; CAD97091 ; Mb2238 .
    GeneIDi 1091362.
    KEGGi mbo:Mb2238.
    PATRICi 18006616. VBIMycBov88188_2454.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281564.
    KOi K00658.
    OMAi QEDETVE.

    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.
    IPR014276. 2-oxoglutarate_DH_E2.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsi TIGR02927. SucB_Actino. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-935 / AF2122/97.

    Entry informationi

    Entry nameiODP2_MYCBO
    AccessioniPrimary (citable) accession number: P65634
    Secondary accession number(s): Q10381, X2BJM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3