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Protein

Polyamine aminopropyltransferase

Gene

speE

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. It has lower affinity and lower activity towards 1,3-diaminopropane, cadaverine (1,5-diaminopentane), agmatine, norspermidine and spermidine (in vitro).UniRule annotation2 Publications

Catalytic activityi

S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.UniRule annotation2 Publications

Enzyme regulationi

Strongly inhibited by S-adenosyl-1,8-diamino-3-thiooctane.1 Publication

Kineticsi

Kcat is 0.77 sec(-1) for aminopropyltransferase activity with putrescine as substrate (at pH 7.5 and 37 degrees Celsius). Kcat is 22.7 sec(-1) for aminopropyltransferase activity with putrescine as substrate (at pH 7.5 and 80 degrees Celsius).1 Publication

  1. KM=0.75 µM for S-adenosylmethioninamine (at pH 7.5 and 37 degrees Celsius)1 Publication
  2. KM=19 µM for putrescine (at pH 7.5 and 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius.1 Publication

    Pathwayi: spermidine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes spermidine from putrescine.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Polyamine aminopropyltransferase (speE)
    This subpathway is part of the pathway spermidine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes spermidine from putrescine, the pathway spermidine biosynthesis and in Amine and polyamine biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 211PolyamineUniRule annotation
    Binding sitei46 – 461S-adenosylmethioninamine1 Publication
    Binding sitei66 – 661Polyamine; via carbonyl oxygenUniRule annotation
    Binding sitei77 – 771Polyamine1 Publication
    Binding sitei101 – 1011Polyamine1 Publication
    Binding sitei121 – 1211S-adenosylmethioninamine1 Publication
    Active sitei170 – 1701Proton acceptor1 Publication

    GO - Molecular functioni

    • agmatine aminopropyltransferase activity Source: UniProtKB
    • cadaverine aminopropyltransferase activity Source: UniProtKB
    • spermidine synthase activity Source: UniProtKB
    • sym-norspermidine synthase activity Source: UniProtKB
    • thermospermine synthase activity Source: UniProtKB

    GO - Biological processi

    • spermidine biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Polyamine biosynthesis, Spermidine biosynthesis

    Enzyme and pathway databases

    BioCyciTMAR243274:GC6P-679-MONOMER.
    BRENDAi2.5.1.16. 6331.
    UniPathwayiUPA00248; UER00314.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyamine aminopropyltransferase1 PublicationUniRule annotation
    Alternative name(s):
    Putrescine aminopropyltransferase1 PublicationUniRule annotation
    Short name:
    PAPT1 PublicationUniRule annotation
    Spermidine synthase1 PublicationUniRule annotation (EC:2.5.1.16UniRule annotation2 Publications)
    Short name:
    SPDS1 PublicationUniRule annotation
    Short name:
    SPDSY1 PublicationUniRule annotation
    Gene namesi
    Name:speEUniRule annotation
    Ordered Locus Names:TM_0654
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    Proteomesi
    • UP000008183 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi76 – 761Y → F: Reduces enzyme activity about 1000-fold. 1 Publication
    Mutagenesisi101 – 1011D → I: Reduces enzyme activity over 10000-fold. 1 Publication
    Mutagenesisi170 – 1701D → A: Reduces enzyme activity over 10000-fold. 1 Publication
    Mutagenesisi173 – 1731D → A: Reduces enzyme activity about 500-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 296296Polyamine aminopropyltransferasePRO_0000156513Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi243274.TM0654.

    Structurei

    Secondary structure

    1
    296
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74Combined sources
    Beta strandi15 – 228Combined sources
    Beta strandi26 – 338Combined sources
    Beta strandi35 – 428Combined sources
    Beta strandi47 – 537Combined sources
    Turni54 – 563Combined sources
    Beta strandi57 – 626Combined sources
    Beta strandi65 – 695Combined sources
    Turni70 – 723Combined sources
    Helixi73 – 8715Combined sources
    Beta strandi88 – 903Combined sources
    Beta strandi93 – 986Combined sources
    Helixi103 – 1086Combined sources
    Beta strandi115 – 1228Combined sources
    Helixi124 – 13310Combined sources
    Helixi135 – 1384Combined sources
    Helixi139 – 1424Combined sources
    Beta strandi146 – 1516Combined sources
    Helixi153 – 1564Combined sources
    Helixi157 – 1593Combined sources
    Beta strandi164 – 1707Combined sources
    Helixi177 – 1793Combined sources
    Helixi181 – 1833Combined sources
    Helixi185 – 19410Combined sources
    Beta strandi195 – 20410Combined sources
    Turni208 – 2114Combined sources
    Helixi212 – 22514Combined sources
    Beta strandi227 – 2359Combined sources
    Beta strandi242 – 25211Combined sources
    Turni255 – 2584Combined sources
    Helixi261 – 2655Combined sources
    Helixi276 – 2816Combined sources
    Helixi287 – 2926Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1INLX-ray1.50A/B/C/D1-296[»]
    1JQ3X-ray1.80A/B/C/D1-296[»]
    ProteinModelPortaliQ9WZC2.
    SMRiQ9WZC2. Positions 2-296.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WZC2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 251236PABSUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 1532S-adenosylmethioninamine binding1 Publication
    Regioni171 – 1733Polyamine binding1 Publication

    Sequence similaritiesi

    Belongs to the spermidine/spermine synthase family.UniRule annotation
    Contains 1 PABS (polyamine biosynthesis) domain.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CCX. Bacteria.
    COG0421. LUCA.
    InParanoidiQ9WZC2.
    KOiK00797.
    OMAiSGLWSFT.
    OrthoDBiEOG644ZMH.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    HAMAPiMF_00198. Spermidine_synth.
    InterProiIPR030374. PABS.
    IPR030373. PABS_CS.
    IPR029063. SAM-dependent_MTases.
    IPR001045. Spermi_synthase.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    TIGRFAMsiTIGR00417. speE. 1 hit.
    PROSITEiPS01330. PABS_1. 1 hit.
    PS51006. PABS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9WZC2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRTLKELERE LQPRQHLWYF EYYTGNNVGL FMKMNRVIYS GQSDIQRIDI
    60 70 80 90 100
    FENPDLGVVF ALDGITMTTE KDEFMYHEML AHVPMFLHPN PKKVLIIGGG
    110 120 130 140 150
    DGGTLREVLK HDSVEKAILC EVDGLVIEAA RKYLKQTSCG FDDPRAEIVI
    160 170 180 190 200
    ANGAEYVRKF KNEFDVIIID STDPTAGQGG HLFTEEFYQA CYDALKEDGV
    210 220 230 240 250
    FSAETEDPFY DIGWFKLAYR RISKVFPITR VYLGFMTTYP SGMWSYTFAS
    260 270 280 290
    KGIDPIKDFD PEKVRKFNKE LKYYNEEVHV ASFALPNFVK KELGLM
    Length:296
    Mass (Da):34,142
    Last modified:November 1, 1999 - v1
    Checksum:i9298A156B7481945
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35738.1.
    PIRiC72348.
    RefSeqiNP_228463.1. NC_000853.1.
    WP_010865176.1. NC_000853.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35738; AAD35738; TM_0654.
    GeneIDi897762.
    KEGGitma:TM0654.
    tmi:THEMA_01395.
    PATRICi23936222. VBITheMar51294_0664.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35738.1.
    PIRiC72348.
    RefSeqiNP_228463.1. NC_000853.1.
    WP_010865176.1. NC_000853.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1INLX-ray1.50A/B/C/D1-296[»]
    1JQ3X-ray1.80A/B/C/D1-296[»]
    ProteinModelPortaliQ9WZC2.
    SMRiQ9WZC2. Positions 2-296.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243274.TM0654.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD35738; AAD35738; TM_0654.
    GeneIDi897762.
    KEGGitma:TM0654.
    tmi:THEMA_01395.
    PATRICi23936222. VBITheMar51294_0664.

    Phylogenomic databases

    eggNOGiENOG4105CCX. Bacteria.
    COG0421. LUCA.
    InParanoidiQ9WZC2.
    KOiK00797.
    OMAiSGLWSFT.
    OrthoDBiEOG644ZMH.

    Enzyme and pathway databases

    UniPathwayiUPA00248; UER00314.
    BioCyciTMAR243274:GC6P-679-MONOMER.
    BRENDAi2.5.1.16. 6331.

    Miscellaneous databases

    EvolutionaryTraceiQ9WZC2.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    HAMAPiMF_00198. Spermidine_synth.
    InterProiIPR030374. PABS.
    IPR030373. PABS_CS.
    IPR029063. SAM-dependent_MTases.
    IPR001045. Spermi_synthase.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    TIGRFAMsiTIGR00417. speE. 1 hit.
    PROSITEiPS01330. PABS_1. 1 hit.
    PS51006. PABS_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "Use of aminopropyltransferase inhibitors and of non-metabolizable analogs to study polyamine regulation and function."
      Pegg A.E., Poulin R., Coward J.K.
      Int. J. Biochem. Cell Biol. 27:425-442(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    3. Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-76; ASP-101; ASP-170 AND ASP-173, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
    4. "The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor."
      Korolev S., Ikeguchi Y., Skarina T., Beasley S., Arrowsmith C., Edwards A., Joachimiak A., Pegg A.E., Savchenko A.
      Nat. Struct. Biol. 9:27-31(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF APOENZYME AND COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiSPEE_THEMA
    AccessioniPrimary (citable) accession number: Q9WZC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: December 9, 2015
    This is version 117 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.