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D5U0K8

- D5U0K8_THEAM

UniProt

D5U0K8 - D5U0K8_THEAM

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Thermosphaera aggregans (strain DSM 11486 / M11TL)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.UniRule annotation

    Catalytic activityi

    S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2.UniRule annotation

    Cofactori

    Pyruvoyl group.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei65 – 662Cleavage (non-hydrolytic); by autolysisUniRule annotation
    Active sitei66 – 661Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
    Active sitei71 – 711Proton acceptor; for processing activityUniRule annotation
    Active sitei86 – 861Proton donor; for catalytic activityUniRule annotation

    GO - Molecular functioni

    1. adenosylmethionine decarboxylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. S-adenosylmethioninamine biosynthetic process Source: UniProtKB-HAMAP
    2. spermidine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    DecarboxylaseUniRule annotation, Lyase

    Keywords - Biological processi

    Polyamine biosynthesisUniRule annotation, Spermidine biosynthesisUniRule annotation

    Keywords - Ligandi

    PyruvateUniRule annotation, S-adenosyl-L-methionineUniRule annotation, Schiff baseUniRule annotation

    Enzyme and pathway databases

    BioCyciTAGG633148:GHBI-392-MONOMER.
    UniPathwayiUPA00331; UER00451.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine decarboxylase proenzymeUniRule annotation (EC:4.1.1.50UniRule annotation)
    Short name:
    AdoMetDCUniRule annotation
    Short name:
    SAMDCUniRule annotation
    Gene namesi
    Name:speHUniRule annotation
    Ordered Locus Names:Tagg_0383Imported
    OrganismiThermosphaera aggregans (strain DSM 11486 / M11TL)Imported
    Taxonomic identifieri633148 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeThermosphaera
    ProteomesiUP000002376: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661Pyruvic acid (Ser); by autocatalysisUniRule annotation

    Post-translational modificationi

    Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.UniRule annotation

    Keywords - PTMi

    Autocatalytic cleavageUniRule annotation, ZymogenUniRule annotation

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.UniRule annotation

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000216579.
    KOiK01611.
    OMAiLMAKEHS.

    Family and domain databases

    Gene3Di3.60.90.10. 1 hit.
    HAMAPiMF_00464. AdoMetDC_1.
    InterProiIPR003826. AdoMetDC_fam_prok.
    IPR016067. S-AdoMet_deCO2ase_core.
    IPR017716. S-AdoMet_deCOase_pro-enz.
    [Graphical view]
    PfamiPF02675. AdoMet_dc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56276. SSF56276. 1 hit.
    TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    D5U0K8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTLKKVIGK HVYGEAYQCD PAILSDEKAL EKIVRNAAVE GNLTLLDVKA    50
    WKINPGVSIV GIILESHISI HTWPEYEFAT IDVYTCGSTS DPIKAFKYII 100
    KELKAKKYSM KVSSRDYEEM 120
    Length:120
    Mass (Da):13,540
    Last modified:July 13, 2010 - v1
    Checksum:iC804D8608EEC7C8A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001939 Genomic DNA. Translation: ADG90658.1.
    RefSeqiWP_013129251.1. NC_014160.1.
    YP_003649610.1. NC_014160.1.

    Genome annotation databases

    EnsemblBacteriaiADG90658; ADG90658; Tagg_0383.
    GeneIDi9165396.
    KEGGitag:Tagg_0383.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001939 Genomic DNA. Translation: ADG90658.1 .
    RefSeqi WP_013129251.1. NC_014160.1.
    YP_003649610.1. NC_014160.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADG90658 ; ADG90658 ; Tagg_0383 .
    GeneIDi 9165396.
    KEGGi tag:Tagg_0383.

    Phylogenomic databases

    HOGENOMi HOG000216579.
    KOi K01611.
    OMAi LMAKEHS.

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .
    BioCyci TAGG633148:GHBI-392-MONOMER.

    Family and domain databases

    Gene3Di 3.60.90.10. 1 hit.
    HAMAPi MF_00464. AdoMetDC_1.
    InterProi IPR003826. AdoMetDC_fam_prok.
    IPR016067. S-AdoMet_deCO2ase_core.
    IPR017716. S-AdoMet_deCOase_pro-enz.
    [Graphical view ]
    Pfami PF02675. AdoMet_dc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56276. SSF56276. 1 hit.
    TIGRFAMsi TIGR03330. SAM_DCase_Bsu. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 11486 / M11TLImported.
    2. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: DSM 11486.

    Entry informationi

    Entry nameiD5U0K8_THEAM
    AccessioniPrimary (citable) accession number: D5U0K8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 13, 2010
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3