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Q5JDS7

- SPEH_THEKO

UniProt

Q5JDS7 - SPEH_THEKO

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Thermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      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

    BioCyciTKOD69014:GH72-1624-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:TK1592
    OrganismiThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
    Taxonomic identifieri69014 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    ProteomesiUP000000536: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6565S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_0000030147Add
    BLAST
    Chaini66 – 14378S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_0000030148Add
    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

    STRINGi69014.TK1592.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5JDS7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1586.
    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.

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

    Q5JDS7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEIETIGFH YVVEAAGCDP EVLGNADRIR QIFLEAAKVG NMEVKASYFF    50
    KFSPTGVSGV VIVAESHISV HTWPEKGYAA LDVYTCGTKA NPEKAVDYIL 100
    EQFKAKYAHV SEIKRGIEED DETFTHMIMT WEEALRKNGN GSG 143
    Length:143
    Mass (Da):15,880
    Last modified:February 15, 2005 - v1
    Checksum:i556F2CEABE1E0C71
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006878 Genomic DNA. Translation: BAD85781.1.
    RefSeqiYP_184005.1. NC_006624.1.

    Genome annotation databases

    EnsemblBacteriaiBAD85781; BAD85781; TK1592.
    GeneIDi3234568.
    KEGGitko:TK1592.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006878 Genomic DNA. Translation: BAD85781.1 .
    RefSeqi YP_184005.1. NC_006624.1.

    3D structure databases

    ProteinModelPortali Q5JDS7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 69014.TK1592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD85781 ; BAD85781 ; TK1592 .
    GeneIDi 3234568.
    KEGGi tko:TK1592.

    Phylogenomic databases

    eggNOGi COG1586.
    HOGENOMi HOG000216579.
    KOi K01611.
    OMAi LMAKEHS.

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .
    BioCyci TKOD69014:GH72-1624-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. "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
      Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
      Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-918 / JCM 12380 / KOD1.

    Entry informationi

    Entry nameiSPEH_THEKO
    AccessioniPrimary (citable) accession number: Q5JDS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 65 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