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Q9WZC3

- SPEH_THEMA

UniProt

Q9WZC3 - SPEH_THEMA

Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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.By similarity

    Catalytic activityi

    S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2.

    Cofactori

    Pyruvoyl group.Curated

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei62 – 632Cleavage (non-hydrolytic); by autolysisCurated
    Active sitei63 – 631Schiff-base intermediate with substrate; via pyruvic acidBy similarity
    Active sitei68 – 681Proton acceptor; for processing activity1 Publication
    Active sitei83 – 831Proton donor; for catalytic activity1 Publication

    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

    UniPathwayiUPA00331; UER00451.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.50)
    Short name:
    AdoMetDC
    Short name:
    SAMDC
    Cleaved into the following 2 chains:
    Gene namesi
    Name:speH
    Ordered Locus Names:TM_0655
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551S → A: Cleaves more rapidly than the wild-type. 1 Publication
    Mutagenesisi63 – 631S → A: Loss of processing. 1 Publication
    Mutagenesisi68 – 681H → A: Cleaves much more slowly than the wild-type, but the addition of hydroxylamine which is known to cleave ester bonds leads to the cleavage of this mutant. 1 Publication
    Mutagenesisi83 – 831C → A: Cleaves more rapidly than the wild-type. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6262S-adenosylmethionine decarboxylase beta chainCuratedPRO_0000030123Add
    BLAST
    Chaini63 – 13068S-adenosylmethionine decarboxylase alpha chainCuratedPRO_0000030124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631Pyruvic acid (Ser); by autocatalysisCurated

    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 Probable.Curated

    Keywords - PTMi

    Autocatalytic cleavage, Zymogen

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.1 Publication

    Protein-protein interaction databases

    STRINGi243274.TM0655.

    Structurei

    Secondary structure

    1
    130
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1412
    Helixi17 – 204
    Helixi23 – 3715
    Beta strandi41 – 488
    Beta strandi50 – 523
    Beta strandi54 – 607
    Beta strandi63 – 708
    Helixi71 – 733
    Beta strandi75 – 8410
    Helixi89 – 10012
    Beta strandi103 – 11412
    Helixi115 – 1184

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TLUX-ray1.55A/B1-130[»]
    1TMIX-ray1.70A/B1-130[»]
    1VR7X-ray1.20A/B1-130[»]
    3IWBX-ray2.06A/C64-130[»]
    B/D1-62[»]
    3IWCX-ray1.90A/C64-130[»]
    B/D1-62[»]
    3IWDX-ray1.90A/C64-130[»]
    B/D1-62[»]
    ProteinModelPortaliQ9WZC3.
    SMRiQ9WZC3. Positions 2-121.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WZC3.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1586.
    KOiK01611.
    OMAiINPWDAC.
    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.

    Q9WZC3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSLGRHLVA EFYECDREVL DNVQLIEQEM KQAAYESGAT IVTSTFHRFL    50
    PYGVSGVVVI SESHLTIHTW PEYGYAAIDL FTCGEDVDPW KAFEHLKKAL 100
    KAKRVHVVEH ERGRYDEIGI PEDSPHKAAV 130
    Length:130
    Mass (Da):14,785
    Last modified:November 1, 1999 - v1
    Checksum:i7659FE20A2019928
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35739.1.
    PIRiD72348.
    RefSeqiNP_228464.1. NC_000853.1.
    YP_007977005.1. NC_021214.1.
    YP_008990376.1. NC_023151.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35739; AAD35739; TM_0655.
    GeneIDi897764.
    KEGGitma:TM0655.
    tmi:THEMA_01390.
    tmm:Tmari_0655.
    PATRICi23936224. VBITheMar51294_0665.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35739.1 .
    PIRi D72348.
    RefSeqi NP_228464.1. NC_000853.1.
    YP_007977005.1. NC_021214.1.
    YP_008990376.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TLU X-ray 1.55 A/B 1-130 [» ]
    1TMI X-ray 1.70 A/B 1-130 [» ]
    1VR7 X-ray 1.20 A/B 1-130 [» ]
    3IWB X-ray 2.06 A/C 64-130 [» ]
    B/D 1-62 [» ]
    3IWC X-ray 1.90 A/C 64-130 [» ]
    B/D 1-62 [» ]
    3IWD X-ray 1.90 A/C 64-130 [» ]
    B/D 1-62 [» ]
    ProteinModelPortali Q9WZC3.
    SMRi Q9WZC3. Positions 2-121.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243274.TM0655.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD35739 ; AAD35739 ; TM_0655 .
    GeneIDi 897764.
    KEGGi tma:TM0655.
    tmi:THEMA_01390.
    tmm:Tmari_0655.
    PATRICi 23936224. VBITheMar51294_0665.

    Phylogenomic databases

    eggNOGi COG1586.
    KOi K01611.
    OMAi INPWDAC.
    OrthoDBi EOG6358J6.

    Enzyme and pathway databases

    UniPathwayi UPA00331 ; UER00451 .

    Miscellaneous databases

    EvolutionaryTracei Q9WZC3.

    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 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase."
      Toms A.V., Kinsland C., McCloskey D.E., Pegg A.E., Ealick S.E.
      J. Biol. Chem. 279:33837-33846(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-63, SUBUNIT, SELF-PROCESSING, ACTIVE SITES, MUTAGENESIS OF SER-55; SER-63; HIS-68 AND CYS-83.
    3. "Crystal structure of S-adenosylmethionine decarboxylase proenzyme (tm0655) from Thermotoga maritima at 1.2-A resolution."
      Joint center for structural genomics (JCSG)
      Submitted (MAR-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).

    Entry informationi

    Entry nameiSPEH_THEMA
    AccessioniPrimary (citable) accession number: Q9WZC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 99 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3