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A0R0B0

- ODP1_MYCS2

UniProt

A0R0B0 - ODP1_MYCS2

Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. AceE has reductase activity with pyruvate but does not react with 2-oxoglutarate By similarity.By similarity

    Catalytic activityi

    Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

    Cofactori

    Magnesium.By similarity
    Thiamine pyrophosphate.By similarity

    GO - Molecular functioni

    1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Magnesium, Pyruvate, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciMSME246196:GJ4Y-4322-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component (EC:1.2.4.1)
    Short name:
    PDH E1 component
    Gene namesi
    Name:aceE
    Ordered Locus Names:MSMEG_4323, MSMEI_4223
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 929929Pyruvate dehydrogenase E1 componentPRO_0000396809Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki375 – 375Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Interactioni

    Subunit structurei

    Homodimer. Part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3).By similarity

    Protein-protein interaction databases

    STRINGi246196.MSMEG_4323.

    Structurei

    3D structure databases

    ProteinModelPortaliA0R0B0.
    SMRiA0R0B0. Positions 85-916.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG2609.
    HOGENOMiHOG000115215.
    KOiK00163.
    OMAiLVHLMNT.
    OrthoDBiEOG6BW4TW.

    Family and domain databases

    Gene3Di3.40.50.920. 1 hit.
    3.40.50.970. 2 hits.
    InterProiIPR004660. 2-oxoA_DH_E1.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005474. Transketolase_N.
    [Graphical view]
    PfamiPF00456. Transketolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000156. Pyruvate_dh_E1. 1 hit.
    SUPFAMiSSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    TIGRFAMsiTIGR00759. aceE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A0R0B0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTEFVRQDL AQNSSTAAEP DRVRVIREGV ASYLPDIDTE ETAEWLESFD    50
    ELLERSGPAR ARYLMLRLLE RAGEQRVAIP ALTSTDYVNT IPTELEPWFP 100
    GDEDVERRYR AWIRWNAAIM VHRAQRPGVG VGGHISTYAS SATLYEVGFN 150
    HFFRGKSHPG GGDHVFIQGH ASPGIYARAF LEGRLTTDQL DGFRQEHSHS 200
    GGGLPSYPHP RLMPDFWEFP TVSMGLGPMN AIYQARFNHY LHDRGIKDTS 250
    DQHVWAFLGD GEMDEPESRG LIQVAANEAL DNLTFVINCN LQRLDGPVRG 300
    NGKIIQELES FFRGAGWNVI KVVWGREWDV LLHADRDGAL VNLMNSTPDG 350
    DYQTYKANDG AYVRDHFFGR DPRTKALVAD MSDQEIWNLK RGGHDYRKVY 400
    AAYRAAMEHK GQPTVILAKT IKGYTLGQHF EGRNATHQMK KLALEDLKNF 450
    RDVTRVPVSD AQLEEDPYLP PYYHPGPEAP EIRYLLERRR ALGGFVPSRR 500
    TKSKPLALPG SDTYKALKKG SGSQAVATTM ATVRTFKELL RDKNIGPRIV 550
    PIIPDEARTF GMDSWFPSLK IYNRNGQLYT SVDSELMLAY KESEVGQILH 600
    EGINEAGSTS SFTAVGTSYS THDEPMIPIY IFYSMFGFQR TGDGLWAAAD 650
    QMARGFVLGA TAGRTTLTGE GLQHADGHSL LLASTNPAAV TYDPAFAYEI 700
    AHIIESGLQR MYGEDPENVF FYLTIYNEPY QQPAEPENLD VEALLKGLYL 750
    YRPAPEKRAK SAQILASGVA MPEALRAADL LASDWDVAAD VWSVTSWGEL 800
    NREGVAIEKH RLRHPDEPAG TPHVTSALAD AAGPVIAVSD WMRAVPEQIR 850
    PWVPGTYVTL GTDGFGFSDT RPAARRYFNT DAESVVVAVL QGLARDGEID 900
    ASVAAQAAEQ YRIDDVSAAG VSYADTGSA 929
    Length:929
    Mass (Da):103,077
    Last modified:January 9, 2007 - v1
    Checksum:i5CB137A1D69BFB23
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK72760.1.
    CP001663 Genomic DNA. Translation: AFP40679.1.
    RefSeqiYP_006568974.1. NC_018289.1.
    YP_888598.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK72760; ABK72760; MSMEG_4323.
    AFP40679; AFP40679; MSMEI_4223.
    GeneIDi4531364.
    KEGGimsg:MSMEI_4223.
    msm:MSMEG_4323.
    PATRICi18081001. VBIMycSme59918_4241.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK72760.1 .
    CP001663 Genomic DNA. Translation: AFP40679.1 .
    RefSeqi YP_006568974.1. NC_018289.1.
    YP_888598.1. NC_008596.1.

    3D structure databases

    ProteinModelPortali A0R0B0.
    SMRi A0R0B0. Positions 85-916.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246196.MSMEG_4323.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK72760 ; ABK72760 ; MSMEG_4323 .
    AFP40679 ; AFP40679 ; MSMEI_4223 .
    GeneIDi 4531364.
    KEGGi msg:MSMEI_4223.
    msm:MSMEG_4323.
    PATRICi 18081001. VBIMycSme59918_4241.

    Phylogenomic databases

    eggNOGi COG2609.
    HOGENOMi HOG000115215.
    KOi K00163.
    OMAi LVHLMNT.
    OrthoDBi EOG6BW4TW.

    Enzyme and pathway databases

    BioCyci MSME246196:GJ4Y-4322-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 2 hits.
    InterProi IPR004660. 2-oxoA_DH_E1.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005474. Transketolase_N.
    [Graphical view ]
    Pfami PF00456. Transketolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000156. Pyruvate_dh_E1. 1 hit.
    SUPFAMi SSF52518. SSF52518. 2 hits.
    SSF52922. SSF52922. 1 hit.
    TIGRFAMsi TIGR00759. aceE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
      Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
      Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
      Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
      Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    4. Cited for: PUPYLATION AT LYS-375, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiODP1_MYCS2
    AccessioniPrimary (citable) accession number: A0R0B0
    Secondary accession number(s): I7GD92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 10, 2010
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 59 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, Reference proteome

    External Data

    Dasty 3