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Q2JWR6

- Q2JWR6_SYNJA

UniProt

Q2JWR6 - Q2JWR6_SYNJA

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (07 Mar 2006)
      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 annotationSAAS annotation

    Cofactori

    Pyruvoyl group.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei75 – 762Cleavage (non-hydrolytic); by autolysisUniRule annotation
    Active sitei76 – 761Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
    Active sitei81 – 811Proton acceptor; for processing activityUniRule annotation
    Active sitei96 – 961Proton 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 annotationSAAS annotation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciSSP321327:GHFX-570-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:CYA_0574Imported
    OrganismiSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)Imported
    Taxonomic identifieri321327 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000008818: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761Pyruvic 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

    Protein-protein interaction databases

    STRINGi321327.CYA_0574.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2JWR6.
    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.

    Q2JWR6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLHTLSGQLG DRSLALIGIH CILELYDCPA KLLDDVSLVQ QALREAARRS    50
    NSTLLGELCH PFEPQGITAL ALLGESHISI HTWPEAGYAA VDVFTCGRHT 100
    RPEAACEYLI QVFQARRYSL RKLPRRTTDA APIEEMADFP KALSCETAGR 150
    RR 152
    Length:152
    Mass (Da):16,870
    Last modified:March 7, 2006 - v1
    Checksum:i8A9D3D82BB8AF51A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000239 Genomic DNA. Translation: ABC98790.1.
    RefSeqiWP_011429477.1. NC_007775.1.
    YP_474053.1. NC_007775.1.

    Genome annotation databases

    EnsemblBacteriaiABC98790; ABC98790; CYA_0574.
    GeneIDi3897371.
    KEGGicya:CYA_0574.
    PATRICi23809415. VBISynSp90045_0572.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000239 Genomic DNA. Translation: ABC98790.1 .
    RefSeqi WP_011429477.1. NC_007775.1.
    YP_474053.1. NC_007775.1.

    3D structure databases

    ProteinModelPortali Q2JWR6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 321327.CYA_0574.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABC98790 ; ABC98790 ; CYA_0574 .
    GeneIDi 3897371.
    KEGGi cya:CYA_0574.
    PATRICi 23809415. VBISynSp90045_0572.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .
    BioCyci SSP321327:GHFX-570-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. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
      Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
      ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JA-3-3AbImported.

    Entry informationi

    Entry nameiQ2JWR6_SYNJA
    AccessioniPrimary (citable) accession number: Q2JWR6
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 7, 2006
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3