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Q59638

- ODP2_PSEAE

UniProt

Q59638 - ODP2_PSEAE

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (08 Dec 2000)
      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).

    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 sitei520 – 5201Sequence 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

    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:aceF
    Synonyms:aceB
    Ordered Locus Names:PA5016
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA5016.

    Subcellular locationi

    GO - Cellular componenti

    1. pyruvate dehydrogenase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 547547Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162283Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411N6-lipoyllysineBy similarity
    Modified residuei159 – 1591N6-lipoyllysineBy similarity

    2D gel databases

    World-2DPAGE0008:Q59638.

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Protein-protein interaction databases

    STRINGi208964.PA5016.

    Structurei

    3D structure databases

    ProteinModelPortaliQ59638.
    SMRiQ59638. Positions 2-81, 119-198, 305-547.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7474Lipoyl-binding 1Add
    BLAST
    Domaini120 – 19273Lipoyl-binding 2Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl, Repeat

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281562.
    KOiK00627.
    OMAiTEIMVAV.
    PhylomeDBiQ59638.

    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.
    IPR006256. AcTrfase_Pyrv_DH_cplx.
    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.
    TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q59638-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSELIRVPDI GNGEGEVIEL LVKPGDKVEA DQSLLTLESD KASMEIPSPK    50
    AGVVKSIKAK VGDTLKEGDE ILELEVEGGE QPAEAKAEAA PAQPEAPKAE 100
    APAPAPSESK PAAPAAASVQ DIKVPDIGSA GKANVIEVMV KAGDTVEADQ 150
    SLITLESDKA SMEIPSPASG VVESVSIKVG DEVGTGDLIL KLKVEGAAPA 200
    AEEQPAAAPA QAAAPAAEQK PAAAAPAPAK ADTPAPVGAP SRDGAKVHAG 250
    PAVRMLAREF GVELSEVKAS GPKGRILKED VQVFVKEQLQ RAKSGGAGAT 300
    GGAGIPPIPE VDFSKFGEVE EVAMTRLMQV GAANLHRSWL NVPHVTQFDQ 350
    SDITDMEAFR VAQKAAAEKA GVKLTVLPIL LKACAHLLKE LPDFNSSLAP 400
    SGKALIRKKY VHIGFAVDTP DGLLVPVIRD VDRKSLLQLA AEAADLADKA 450
    RNKKLSADAM QGACFTISSL GHIGGTGFTP IVNAPEVAIL GVSKATMQPV 500
    WDGKAFQPRL MLPLSLSYDH RVINGAAAAR FTKRLGELLA DIRTLLL 547
    Length:547
    Mass (Da):56,709
    Last modified:December 8, 2000 - v2
    Checksum:i24E15CCC9A590CB4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti225 – 2251A → V in AAC45354. (PubMed:9171401)Curated
    Sequence conflicti295 – 3017GGAGATG → AVPAPR in AAC45354. (PubMed:9171401)Curated
    Sequence conflicti328 – 3292MQ → IE in AAC45354. (PubMed:9171401)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U47920 Genomic DNA. Translation: AAC45354.1.
    AE004091 Genomic DNA. Translation: AAG08401.1.
    PIRiH83018.
    RefSeqiNP_253703.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG08401; AAG08401; PA5016.
    GeneIDi881297.
    KEGGipae:PA5016.
    PATRICi19844857. VBIPseAer58763_5257.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U47920 Genomic DNA. Translation: AAC45354.1 .
    AE004091 Genomic DNA. Translation: AAG08401.1 .
    PIRi H83018.
    RefSeqi NP_253703.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali Q59638.
    SMRi Q59638. Positions 2-81, 119-198, 305-547.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA5016.

    2D gel databases

    World-2DPAGE 0008:Q59638.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG08401 ; AAG08401 ; PA5016 .
    GeneIDi 881297.
    KEGGi pae:PA5016.
    PATRICi 19844857. VBIPseAer58763_5257.

    Organism-specific databases

    PseudoCAPi PA5016.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281562.
    KOi K00627.
    OMAi TEIMVAV.
    PhylomeDBi Q59638.

    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.
    IPR006256. AcTrfase_Pyrv_DH_cplx.
    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 TIGR01348. PDHac_trf_long. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa."
      Rae J.L., Cutfield J.F., Lamont I.L.
      J. Bacteriol. 179:3561-3571(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: PAO.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiODP2_PSEAE
    AccessioniPrimary (citable) accession number: Q59638
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 8, 2000
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3