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P75392

- ODP2_MYCPN

UniProt

P75392 - ODP2_MYCPN

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei374 – 3741Sequence Analysis

    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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-584.
    MPNE272634:GJ6Z-413-MONOMER.

    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
    E2
    Gene namesi
    Name:pdhC
    Ordered Locus Names:MPN_391
    ORF Names:MP447
    OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
    Taxonomic identifieri272634 [NCBI]
    Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
    ProteomesiUP000000808: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 402402Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162282Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-lipoyllysineBy similarity

    Proteomic databases

    PaxDbiP75392.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

    Protein-protein interaction databases

    IntActiP75392. 1 interaction.
    STRINGi272634.MPN391.

    Structurei

    3D structure databases

    ProteinModelPortaliP75392.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7676Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl

    Phylogenomic databases

    eggNOGiCOG0508.
    KOiK00627.
    OMAiFWHVSEG.
    OrthoDBiEOG610413.

    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.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P75392-1 [UniParc]FASTAAdd to Basket

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    MANEFKFTDV GEGLHEGKVT EILKKVGDTI KVDEALFVVE TDKVTTELPS    50
    PYAGVITAIT TNVGDVVHIG QVMAVIDDGA GAAAPAAPQP VSAPAPAPTP 100
    TFTPTPAPVT TEPVVEEAGA SVVGEIKVSN SVFPIFGVQP SAPQPTPAPV 150
    VQPTSAPTPT PAPASAAAPS GEETIAITTM RKAIAEAMVK SHENIPATIL 200
    TFYVNATKLK QYRESVNGLA LSKYNMKISF FAFFVKAIVN ALKKFPVFNG 250
    RYDKERNLIV LNKDVNVGIA VDTPDGLIVP NIKQAQTKSV VDIAKDIVDL 300
    ANRARSKQIK LPDLSKGTIS VTNFGSLGAA FGTPIIKHPE MCIVATGNME 350
    ERVVRAEGGV AVHTILPLTI AADHRWVDGA DVGRFGKEIA KQIEELIDLE 400
    VA 402
    Length:402
    Mass (Da):42,397
    Last modified:February 1, 1997 - v1
    Checksum:iF09314A9E714A1D6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00089 Genomic DNA. Translation: AAB96095.1.
    PIRiS73773.
    RefSeqiNP_110079.1. NC_000912.1.

    Genome annotation databases

    EnsemblBacteriaiAAB96095; AAB96095; MPN_391.
    GeneIDi877106.
    KEGGimpn:MPN391.
    PATRICi20022158. VBIMycPne110_0422.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00089 Genomic DNA. Translation: AAB96095.1 .
    PIRi S73773.
    RefSeqi NP_110079.1. NC_000912.1.

    3D structure databases

    ProteinModelPortali P75392.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P75392. 1 interaction.
    STRINGi 272634.MPN391.

    Proteomic databases

    PaxDbi P75392.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB96095 ; AAB96095 ; MPN_391 .
    GeneIDi 877106.
    KEGGi mpn:MPN391.
    PATRICi 20022158. VBIMycPne110_0422.

    Phylogenomic databases

    eggNOGi COG0508.
    KOi K00627.
    OMAi FWHVSEG.
    OrthoDBi EOG610413.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-584.
    MPNE272634:GJ6Z-413-MONOMER.

    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.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
      Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
      Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29342 / M129.

    Entry informationi

    Entry nameiODP2_MYCPN
    AccessioniPrimary (citable) accession number: P75392
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 86 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

    Documents

    1. Mycoplasma pneumoniae
      Mycoplasma pneumoniae (strain M129): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3