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A4XJ25

- SPEH_CALS8

UniProt

A4XJ25 - SPEH_CALS8

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (29 May 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
    Sitei62 – 632Cleavage (non-hydrolytic); by autolysisUniRule annotation
    Active sitei63 – 631Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
    Active sitei68 – 681Proton acceptor; for processing activityUniRule annotation
    Active sitei83 – 831Proton 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

    BioCyciCSAC351627:GJ17-1341-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:Csac_1308
    OrganismiCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903)
    Taxonomic identifieri351627 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor
    ProteomesiUP000000256: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6262S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_1000013670Add
    BLAST
    Chaini63 – 12462S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_0000315023Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631Pyruvic 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

    STRINGi351627.Csac_1308.

    Structurei

    3D structure databases

    ProteinModelPortaliA4XJ25.
    SMRiA4XJ25. Positions 3-117.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1586.
    HOGENOMiHOG000216579.
    KOiK01611.
    OMAiHIANMHL.
    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.

    A4XJ25-1 [UniParc]FASTAAdd to Basket

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    MHALGRHIIA ELYGCDKEVL NNRELIEKIM VESALKAGAE VREVAFHKFS    50
    PQGVSGVVVI SESHLTIHTW PELGYAAVDV FTCGERVDPW QACNYITEML 100
    KASHMTTTEV KRGLFEQPVK VANL 124
    Length:124
    Mass (Da):13,837
    Last modified:May 29, 2007 - v1
    Checksum:i4EA13C00427B88B4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000679 Genomic DNA. Translation: ABP66910.1.
    RefSeqiYP_001180101.1. NC_009437.1.

    Genome annotation databases

    EnsemblBacteriaiABP66910; ABP66910; Csac_1308.
    GeneIDi5088248.
    KEGGicsc:Csac_1308.
    PATRICi21252290. VBICalSac56748_1456.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000679 Genomic DNA. Translation: ABP66910.1 .
    RefSeqi YP_001180101.1. NC_009437.1.

    3D structure databases

    ProteinModelPortali A4XJ25.
    SMRi A4XJ25. Positions 3-117.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 351627.Csac_1308.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP66910 ; ABP66910 ; Csac_1308 .
    GeneIDi 5088248.
    KEGGi csc:Csac_1308.
    PATRICi 21252290. VBICalSac56748_1456.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .
    BioCyci CSAC351627:GJ17-1341-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: ATCC 43494 / DSM 8903.

    Entry informationi

    Entry nameiSPEH_CALS8
    AccessioniPrimary (citable) accession number: A4XJ25
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 44 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3