Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A8ALG9

- SPED_CITK8

UniProt

A8ALG9 - SPED_CITK8

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speD

Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (23 Oct 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    BioCyciCKOS290338:GJ8L-3241-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:CKO_03248
    OrganismiCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
    Taxonomic identifieri290338 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter
    ProteomesiUP000008148: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 111111S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_1000013688Add
    BLAST
    Chaini112 – 264153S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_0000315014Add
    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

    PRIDEiA8ALG9.

    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

    STRINGi290338.CKO_03248.

    Structurei

    3D structure databases

    ProteinModelPortaliA8ALG9.
    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.

    A8ALG9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLKLHGFN NLTKSLSFCI YDICYAKTAE ERDGYIAYID ELYNANRLTE    50
    ILSETCSIIG ANILNIARQD YEPQGASVTI LVSEEPVDPQ LIDKTEHPGP 100
    LPEAVVAHLD KSHICVHTYP ESHPEGGLCT FRADIEVSTC GVISPLKALN 150
    YLIHQLESDI VTIDYRVRGF TRDVNGMKHF IDHEINSIQN FMSDDMKSLY 200
    DMVDVNVYQE NIFHTKMLLK EFDLKHYMFH TKPEDLTETE RKEITAALWK 250
    EMREIYYGRN IPAV 264
    Length:264
    Mass (Da):30,367
    Last modified:October 23, 2007 - v1
    Checksum:iEFA8ACA5EE924EA1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000822 Genomic DNA. Translation: ABV14332.1.
    RefSeqiWP_012134037.1. NC_009792.1.
    YP_001454768.1. NC_009792.1.

    Genome annotation databases

    EnsemblBacteriaiABV14332; ABV14332; CKO_03248.
    GeneIDi5583015.
    KEGGicko:CKO_03248.
    PATRICi20389092. VBICitKos71230_2724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000822 Genomic DNA. Translation: ABV14332.1 .
    RefSeqi WP_012134037.1. NC_009792.1.
    YP_001454768.1. NC_009792.1.

    3D structure databases

    ProteinModelPortali A8ALG9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 290338.CKO_03248.

    Proteomic databases

    PRIDEi A8ALG9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABV14332 ; ABV14332 ; CKO_03248 .
    GeneIDi 5583015.
    KEGGi cko:CKO_03248.
    PATRICi 20389092. VBICitKos71230_2724.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .
    BioCyci CKOS290338:GJ8L-3241-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: ATCC BAA-895 / CDC 4225-83 / SGSC4696.

    Entry informationi

    Entry nameiSPED_CITK8
    AccessioniPrimary (citable) accession number: A8ALG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: October 23, 2007
    Last modified: October 1, 2014
    This is version 40 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