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A7GTM8

- SPEH_BACCN

UniProt

A7GTM8 - SPEH_BACCN

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Bacillus cereus subsp. cytotoxis (strain NVH 391-98)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (11 Sep 2007)
      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

    Decarboxylase, Lyase

    Keywords - Biological processi

    Polyamine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Pyruvate, S-adenosyl-L-methionine, Schiff base

    Enzyme and pathway databases

    BioCyciBCYT315749:GH2A-3377-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
    Cleaved into the following 2 chains:
    S-adenosylmethionine decarboxylase beta chainUniRule annotation
    S-adenosylmethionine decarboxylase alpha chainUniRule annotation
    Gene namesi
    Name:speHUniRule annotation
    Ordered Locus Names:Bcer98_3267
    OrganismiBacillus cereus subsp. cytotoxis (strain NVH 391-98)
    Taxonomic identifieri315749 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000002300: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6565S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_1000081168Add
    BLAST
    Chaini66 – 13065S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_1000081169Add
    BLAST

    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 cleavage, Zymogen

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi315749.Bcer98_3267.

    Structurei

    3D structure databases

    ProteinModelPortaliA7GTM8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1586.
    HOGENOMiHOG000216579.
    KOiK01611.
    OMAiGNLYGCN.
    OrthoDBiEOG6358J6.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A7GTM8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTMDTMGRH VIAELWDCDF DKLNDMPFIE QLFVDAALRA GAEVREVAFH    50
    KFAPQGVSGV VIISESHLTI HSFPEHGYAS IDVYTCGDRI DPNVAAEYIA 100
    EGLNAKTRES IELPRGTGSF EIKQRETKAL 130
    Length:130
    Mass (Da):14,471
    Last modified:September 11, 2007 - v1
    Checksum:i12AD847064A61956
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000764 Genomic DNA. Translation: ABS23486.1.
    RefSeqiYP_001376481.1. NC_009674.1.

    Genome annotation databases

    EnsemblBacteriaiABS23486; ABS23486; Bcer98_3267.
    GeneIDi5346012.
    KEGGibcy:Bcer98_3267.
    PATRICi18935176. VBIBacCyt128034_3429.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000764 Genomic DNA. Translation: ABS23486.1 .
    RefSeqi YP_001376481.1. NC_009674.1.

    3D structure databases

    ProteinModelPortali A7GTM8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 315749.Bcer98_3267.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABS23486 ; ABS23486 ; Bcer98_3267 .
    GeneIDi 5346012.
    KEGGi bcy:Bcer98_3267.
    PATRICi 18935176. VBIBacCyt128034_3429.

    Phylogenomic databases

    eggNOGi COG1586.
    HOGENOMi HOG000216579.
    KOi K01611.
    OMAi GNLYGCN.
    OrthoDBi EOG6358J6.

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .
    BioCyci BCYT315749:GH2A-3377-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: NVH 391-98.

    Entry informationi

    Entry nameiSPEH_BACCN
    AccessioniPrimary (citable) accession number: A7GTM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 49 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

    Documents

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

    External Data

    Dasty 3