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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

Manual assertion based on experiment ini

  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), 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)DescriptionActionsGraphical viewLength
    Binding sitei21PolyamineUniRule annotation1
    Binding sitei46S-adenosylmethioninamine1 Publication1
    Binding sitei66Polyamine; via carbonyl oxygenUniRule annotation1
    Binding sitei77Polyamine1 Publication1
    Binding sitei101Polyamine1 Publication1
    Binding sitei121S-adenosylmethioninamine1 Publication1
    Active sitei170Proton acceptor1 Publication1

    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

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi76Y → F: Reduces enzyme activity about 1000-fold. 1 Publication1
    Mutagenesisi101D → I: Reduces enzyme activity over 10000-fold. 1 Publication1
    Mutagenesisi170D → A: Reduces enzyme activity over 10000-fold. 1 Publication1
    Mutagenesisi173D → A: Reduces enzyme activity about 500-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001565131 – 296Polyamine aminopropyltransferaseAdd BLAST296

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi243274.TM0654.

    Structurei

    Secondary structure

    1296
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 7Combined sources4
    Beta strandi15 – 22Combined sources8
    Beta strandi26 – 33Combined sources8
    Beta strandi35 – 42Combined sources8
    Beta strandi47 – 53Combined sources7
    Turni54 – 56Combined sources3
    Beta strandi57 – 62Combined sources6
    Beta strandi65 – 69Combined sources5
    Turni70 – 72Combined sources3
    Helixi73 – 87Combined sources15
    Beta strandi88 – 90Combined sources3
    Beta strandi93 – 98Combined sources6
    Helixi103 – 108Combined sources6
    Beta strandi115 – 122Combined sources8
    Helixi124 – 133Combined sources10
    Helixi135 – 138Combined sources4
    Helixi139 – 142Combined sources4
    Beta strandi146 – 151Combined sources6
    Helixi153 – 156Combined sources4
    Helixi157 – 159Combined sources3
    Beta strandi164 – 170Combined sources7
    Helixi177 – 179Combined sources3
    Helixi181 – 183Combined sources3
    Helixi185 – 194Combined sources10
    Beta strandi195 – 204Combined sources10
    Turni208 – 211Combined sources4
    Helixi212 – 225Combined sources14
    Beta strandi227 – 235Combined sources9
    Beta strandi242 – 252Combined sources11
    Turni255 – 258Combined sources4
    Helixi261 – 265Combined sources5
    Helixi276 – 281Combined sources6
    Helixi287 – 292Combined sources6

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9WZC2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini16 – 251PABSUniRule annotationAdd BLAST236

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni152 – 153S-adenosylmethioninamine binding1 Publication2
    Regioni171 – 173Polyamine binding1 Publication3

    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.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    HAMAPiMF_00198. Spermidine_synth. 1 hit.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1INLX-ray1.50A/B/C/D1-296[»]
    1JQ3X-ray1.80A/B/C/D1-296[»]
    ProteinModelPortaliQ9WZC2.
    SMRiQ9WZC2.
    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.

    Enzyme and pathway databases

    UniPathwayiUPA00248; UER00314.
    BRENDAi2.5.1.16. 6331.

    Miscellaneous databases

    EvolutionaryTraceiQ9WZC2.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    HAMAPiMF_00198. Spermidine_synth. 1 hit.
    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...

    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: November 2, 2016
    This is version 120 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.