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Protein

Polyamine aminopropyltransferase

Gene

speE

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to various amine acceptors such as agmatine, cadaverine (1,5-diaminopentane), putrescine (1,4-diaminobutane) and 1,3-diaminopropane. The biosynthesis of norspermine and thermospermine from sym-norspermidine and spermidine has been also observed, but with a very low activity. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet.1 Publication

Catalytic activityi

S-adenosyl 3-(methylthio)propylamine + 1,5-diaminopentane = S-methyl-5'-thioadenosine + N-(3-aminopropyl)-1,5-diaminopentane.1 Publication
S-adenosylmethioninamine + agmatine = S-methyl-5'-thioadenosine + N(1)-(3-aminopropyl)agmatine.1 Publication
S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.UniRule annotation1 Publication
S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine.1 Publication

Kineticsi

Kcat is 2.09 sec(-1) for aminopropyl transferase activity with cadaverine as amine acceptor. Kcat is 0.18 sec(-1) for aminopropyl transferase activity with putrescine as amine acceptor. Kcat is 0.1 sec(-1) for aminopropyl transferase activity with agmatine as amine acceptor. Kcat is 0.06 sec(-1) for aminopropyl transferase activity with 1,3-diaminopropane as amine acceptor.1 Publication

  1. KM=7.6 µM for agmatine1 Publication
  2. KM=1877 µM for 1,3-diaminopropane1 Publication
  3. KM=3767 µM for cadaverine1 Publication
  4. KM=7703 µM for putrescine1 Publication

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius. The enzyme is highly thermophilic. 50% activity is still observable at 103 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 sitei7 – 71PolyamineUniRule annotation
    Binding sitei31 – 311S-adenosylmethioninamineUniRule annotation
    Binding sitei62 – 621PolyamineUniRule annotation
    Binding sitei86 – 861PolyamineUniRule annotation
    Binding sitei105 – 1051S-adenosylmethioninamineUniRule annotation
    Active sitei159 – 1591Proton acceptorUniRule annotation
    Binding sitei166 – 1661S-adenosylmethioninamide; via carbonyl oxygen

    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

    • polyamine biosynthetic process Source: UniProtKB
    • spermidine biosynthetic process Source: UniProtKB-HAMAP
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Polyamine biosynthesis, Spermidine biosynthesis

    Enzyme and pathway databases

    BRENDAi2.5.1.104. 5243.
    SABIO-RKQ8U4G1.
    UniPathwayiUPA00248; UER00314.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyamine aminopropyltransferase1 PublicationUniRule annotation
    Alternative name(s):
    1,3-diaminopropane aminopropyltransferase1 Publication (EC:2.5.1.231 Publication)
    Agmatine aminopropyltransferase1 Publication
    Agmatine/cadaverine aminopropyltransferase1 Publication
    Cadaverine aminopropyltransferase1 Publication (EC:2.5.1.-1 Publication)
    N(1)-aminopropylagmatine synthase1 Publication (EC:2.5.1.1041 Publication)
    Putrescine aminopropyltransferaseUniRule annotation1 Publication (EC:2.5.1.16UniRule annotation1 Publication)
    Short name:
    PAPTUniRule annotation
    Spermidine synthaseUniRule annotation1 Publication
    Short name:
    SPDSUniRule annotation
    Short name:
    SPDSYUniRule annotation
    Sym-norspermidine synthase1 Publication
    Gene namesi
    Name:speEUniRule annotation
    Ordered Locus Names:PF0127
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000001013 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 281281Polyamine aminopropyltransferasePRO_0000156530Add
    BLAST

    Proteomic databases

    PRIDEiQ8U4G1.

    Expressioni

    Inductioni

    At temperatures higher than 95 degrees Celsius or by oxidative shock.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi186497.PF0127.

    Structurei

    Secondary structure

    1
    281
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95Combined sources
    Helixi10 – 123Combined sources
    Beta strandi13 – 175Combined sources
    Beta strandi19 – 279Combined sources
    Beta strandi32 – 4110Combined sources
    Beta strandi43 – 475Combined sources
    Beta strandi50 – 545Combined sources
    Turni55 – 584Combined sources
    Helixi59 – 7214Combined sources
    Beta strandi78 – 836Combined sources
    Helixi88 – 936Combined sources
    Beta strandi99 – 1068Combined sources
    Helixi108 – 11710Combined sources
    Turni120 – 1234Combined sources
    Helixi124 – 1296Combined sources
    Beta strandi134 – 1418Combined sources
    Helixi143 – 1497Combined sources
    Beta strandi153 – 1597Combined sources
    Helixi173 – 18210Combined sources
    Beta strandi183 – 19513Combined sources
    Turni196 – 1983Combined sources
    Helixi200 – 21314Combined sources
    Beta strandi215 – 2228Combined sources
    Beta strandi227 – 24014Combined sources
    Helixi248 – 2525Combined sources
    Helixi261 – 2688Combined sources
    Helixi272 – 2787Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MJFX-ray1.80A/B1-281[»]
    ProteinModelPortaliQ8U4G1.
    SMRiQ8U4G1. Positions 4-279.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8U4G1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 238233PABSUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 522Polyamine bindingUniRule annotation
    Regioni142 – 1432S-adenosylmethioninamine bindingUniRule annotation
    Regioni160 – 1623Polyamine bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiarCOG00050. Archaea.
    COG0421. LUCA.
    HOGENOMiHOG000256146.
    KOiK00797.
    OMAiRSYHEPL.

    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.

    Q8U4G1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MERAFIEWYP RGYGVAFKIK KKIYEKLSKY QKIEVYETEG FGRLLALDGT
    60 70 80 90 100
    VQLVTLGERS YHEPLVHPAM LAHPKPKRVL VIGGGDGGTV REVLQHDVDE
    110 120 130 140 150
    VIMVEIDEDV IMVSKDLIKI DNGLLEAMLN GKHEKAKLTI GDGFEFIKNN
    160 170 180 190 200
    RGFDVIIADS TDPVGPAKVL FSEEFYRYVY DALNNPGIYV TQAGSVYLFT
    210 220 230 240 250
    DELISAYKEM KKVFDRVYYY SFPVIGYASP WAFLVGVKGD IDFTKIDRER
    260 270 280
    AKKLQLEYYD PLMHETLFQM PKYIRETLQR L
    Length:281
    Mass (Da):32,334
    Last modified:June 1, 2002 - v1
    Checksum:i72C97AE45BE1C487
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80251.1.
    RefSeqiWP_011011239.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80251; AAL80251; PF0127.
    GeneIDi1467956.
    KEGGipfu:PF0127.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80251.1.
    RefSeqiWP_011011239.1. NC_003413.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MJFX-ray1.80A/B1-281[»]
    ProteinModelPortaliQ8U4G1.
    SMRiQ8U4G1. Positions 4-279.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi186497.PF0127.

    Proteomic databases

    PRIDEiQ8U4G1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL80251; AAL80251; PF0127.
    GeneIDi1467956.
    KEGGipfu:PF0127.

    Phylogenomic databases

    eggNOGiarCOG00050. Archaea.
    COG0421. LUCA.
    HOGENOMiHOG000256146.
    KOiK00797.
    OMAiRSYHEPL.

    Enzyme and pathway databases

    UniPathwayiUPA00248; UER00314.
    BRENDAi2.5.1.104. 5243.
    SABIO-RKQ8U4G1.

    Miscellaneous databases

    EvolutionaryTraceiQ8U4G1.

    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_PYRFU
    AccessioniPrimary (citable) accession number: Q8U4G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: June 1, 2002
    Last modified: September 7, 2016
    This is version 95 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, Direct protein sequencing, 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.