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Q59695

- ACOC_PSEPU

UniProt

Q59695 - ACOC_PSEPU

Protein

Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system

Gene

acoC

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetoin catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Acetoin catabolism

    Enzyme and pathway databases

    UniPathwayiUPA00040.

    Protein family/group databases

    MEROPSiS33.010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system (EC:2.3.1.12)
    Alternative name(s):
    Acetoin dehydrogenase E2 component
    Dihydrolipoamide acetyltransferase component of acetoin cleaving system
    Gene namesi
    Name:acoC
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving systemPRO_0000162305Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei45 – 451N6-lipoyllysineBy similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ59695.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7878Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000089. Biotin_lipoyl.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00364. Biotin_lipoyl. 1 hit.
    [Graphical view]
    PRINTSiPR00111. ABHYDROLASE.
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q59695-1 [UniParc]FASTAAdd to Basket

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    MSQIHTLTMP KWGLSMTEGR VDAWLKQEGD EINKGDEVLD VETDKISSSV    50
    EAPFSGVLRR QVAKPDETLP VGALLAVVVE GEAEESEIDA VVQRFQAEFV 100
    AEGGADQAQG PAPQKAEVGG RLLRWFELGG EGGTPLVLVH GFGGDLNNWL 150
    FNHPALAAER RVIALDLPGH GESAKALQRG DLDELSETVL ALLDHLDIAK 200
    AHLAGHSMGG AVSLNVAGLA PQRVASLSLI ASAGLGEAIN GQYLQGFVAA 250
    ANRNALKPQM VQLFADPALV TRQMLEDMLK FKRLEGVDEA LRQLALAIAD 300
    GDRQRHDLRS VLGQHPALVV WGGKDAIIPA SHARKGPEAE VLVLPEAGHM 350
    VQMEAAEQVN QQMLAFLRKH 370
    Length:370
    Mass (Da):39,638
    Last modified:November 1, 1996 - v1
    Checksum:iF3DFA23B14983B9F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35343 Genomic DNA. Translation: AAB58981.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35343 Genomic DNA. Translation: AAB58981.1 .

    3D structure databases

    ProteinModelPortali Q59695.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S33.010.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00040 .

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000089. Biotin_lipoyl.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00364. Biotin_lipoyl. 1 hit.
    [Graphical view ]
    PRINTSi PR00111. ABHYDROLASE.
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF53474. SSF53474. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway."
      Huang M., Oppermann F.B., Steinbuchel A.
      FEMS Microbiol. Lett. 124:141-150(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: G2.

    Entry informationi

    Entry nameiACOC_PSEPU
    AccessioniPrimary (citable) accession number: Q59695
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3