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Q8ZBJ7

- SPED_YERPE

UniProt

Q8ZBJ7 - SPED_YERPE

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speD

Organism
Yersinia pestis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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
    Sitei111 – 1122Cleavage (non-hydrolytic); by autolysisUniRule annotation
    Active sitei112 – 1121Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
    Active sitei117 – 1171Proton acceptor; for processing activityUniRule annotation
    Active sitei140 – 1401Proton 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

    BioCyciYPES214092:GKDD-3366-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:speDUniRule annotation
    Ordered Locus Names:YPO3412, y0774, YP_0273
    OrganismiYersinia pestis
    Taxonomic identifieri632 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000000815: Chromosome, UP000001019: Chromosome, UP000002490: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 111111S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_0000030075Add
    BLAST
    Chaini112 – 264153S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_0000030076Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei112 – 1121Pyruvic 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

    Proteomic databases

    PRIDEiQ8ZBJ7.

    Interactioni

    Subunit structurei

    Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.UniRule annotation

    Protein-protein interaction databases

    STRINGi214092.YPO3412.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8ZBJ7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1586.
    HOGENOMiHOG000116821.
    KOiK01611.
    OMAiVKHYIDH.
    OrthoDBiEOG68Q0SQ.

    Family and domain databases

    Gene3Di3.60.90.10. 1 hit.
    HAMAPiMF_00465. AdoMetDC_2.
    InterProiIPR003826. AdoMetDC_fam_prok.
    IPR009165. S-AdoMet_deCO2ase_bac.
    IPR016067. S-AdoMet_deCO2ase_core.
    [Graphical view]
    PfamiPF02675. AdoMet_dc. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001356. SAM_decarboxylas. 1 hit.
    SUPFAMiSSF56276. SSF56276. 2 hits.
    TIGRFAMsiTIGR03331. SAM_DCase_Eco. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q8ZBJ7-1 [UniParc]FASTAAdd to Basket

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    MSKLKLHGFN NLTKSLSFCI YDICYAKTAD DRDGYIAYID EQYNANRLTE    50
    ILSETCSIIG ANILNIARQD YDPQGASVTI LVSEEPVDPR DVDTSEHPGP 100
    LPSAVVAHLD KSHICVHTYP ESHPEAGLCT FRADIEVSTC GVISPLKALN 150
    YLIHQLESDI VTMDYRVRGF TRDINGVKHF IDHKINSIQN FMSDDMKSLY 200
    HMMDVNVYQE NIFHTKMMLK DFDLKHYLFN AKPEELSAEE KEQITRLLYK 250
    EMQEIYYGRN VPEV 264
    Length:264
    Mass (Da):30,293
    Last modified:March 1, 2002 - v1
    Checksum:iE4C0AEE946FEDC89
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL590842 Genomic DNA. Translation: CAL22001.1.
    AE009952 Genomic DNA. Translation: AAM84361.1.
    AE017042 Genomic DNA. Translation: AAS60549.1.
    PIRiAF0414.
    RefSeqiNP_668110.1. NC_004088.1.
    NP_991672.1. NC_005810.1.
    YP_002348304.1. NC_003143.1.

    Genome annotation databases

    EnsemblBacteriaiAAM84361; AAM84361; y0774.
    AAS60549; AAS60549; YP_0273.
    GeneIDi1145721.
    1176229.
    2766455.
    KEGGiype:YPO3412.
    ypk:y0774.
    ypm:YP_0273.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL590842 Genomic DNA. Translation: CAL22001.1 .
    AE009952 Genomic DNA. Translation: AAM84361.1 .
    AE017042 Genomic DNA. Translation: AAS60549.1 .
    PIRi AF0414.
    RefSeqi NP_668110.1. NC_004088.1.
    NP_991672.1. NC_005810.1.
    YP_002348304.1. NC_003143.1.

    3D structure databases

    ProteinModelPortali Q8ZBJ7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 214092.YPO3412.

    Proteomic databases

    PRIDEi Q8ZBJ7.

    Protocols and materials databases

    DNASUi 1145721.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM84361 ; AAM84361 ; y0774 .
    AAS60549 ; AAS60549 ; YP_0273 .
    GeneIDi 1145721.
    1176229.
    2766455.
    KEGGi ype:YPO3412.
    ypk:y0774.
    ypm:YP_0273.

    Phylogenomic databases

    eggNOGi COG1586.
    HOGENOMi HOG000116821.
    KOi K01611.
    OMAi VKHYIDH.
    OrthoDBi EOG68Q0SQ.

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .
    BioCyci YPES214092:GKDD-3366-MONOMER.

    Family and domain databases

    Gene3Di 3.60.90.10. 1 hit.
    HAMAPi MF_00465. AdoMetDC_2.
    InterProi IPR003826. AdoMetDC_fam_prok.
    IPR009165. S-AdoMet_deCO2ase_bac.
    IPR016067. S-AdoMet_deCO2ase_core.
    [Graphical view ]
    Pfami PF02675. AdoMet_dc. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001356. SAM_decarboxylas. 1 hit.
    SUPFAMi SSF56276. SSF56276. 2 hits.
    TIGRFAMsi TIGR03331. SAM_DCase_Eco. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CO-92 / Biovar Orientalis.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KIM10+ / Biovar Mediaevalis.
    3. "Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
      Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R.
      , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
      DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 91001 / Biovar Mediaevalis.

    Entry informationi

    Entry nameiSPED_YERPE
    AccessioniPrimary (citable) accession number: Q8ZBJ7
    Secondary accession number(s): Q0WBN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 91 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