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Protein

Polyamine aminopropyltransferase

Gene

speE

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: -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 + N1-(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)DescriptionActionsGraphical viewLength
    Binding sitei7PolyamineUniRule annotation1
    Binding sitei31S-adenosylmethioninamineUniRule annotation1
    Binding sitei62PolyamineUniRule annotation1
    Binding sitei86PolyamineUniRule annotation1
    Binding sitei105S-adenosylmethioninamineUniRule annotation1
    Active sitei159Proton acceptorUniRule annotation1
    Binding sitei166S-adenosylmethioninamide; via carbonyl oxygen1

    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-UniPathway

    Keywordsi

    Molecular functionTransferase
    Biological processPolyamine biosynthesis, Spermidine biosynthesis

    Enzyme and pathway databases

    BRENDAi2.5.1.104 5243
    SABIO-RKiQ8U4G1
    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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001565301 – 281Polyamine aminopropyltransferaseAdd BLAST281

    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

    1281
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 9Combined sources5
    Helixi10 – 12Combined sources3
    Beta strandi13 – 17Combined sources5
    Beta strandi19 – 27Combined sources9
    Beta strandi32 – 41Combined sources10
    Beta strandi43 – 47Combined sources5
    Beta strandi50 – 54Combined sources5
    Turni55 – 58Combined sources4
    Helixi59 – 72Combined sources14
    Beta strandi78 – 83Combined sources6
    Helixi88 – 93Combined sources6
    Beta strandi99 – 106Combined sources8
    Helixi108 – 117Combined sources10
    Turni120 – 123Combined sources4
    Helixi124 – 129Combined sources6
    Beta strandi134 – 141Combined sources8
    Helixi143 – 149Combined sources7
    Beta strandi153 – 159Combined sources7
    Helixi173 – 182Combined sources10
    Beta strandi183 – 195Combined sources13
    Turni196 – 198Combined sources3
    Helixi200 – 213Combined sources14
    Beta strandi215 – 222Combined sources8
    Beta strandi227 – 240Combined sources14
    Helixi248 – 252Combined sources5
    Helixi261 – 268Combined sources8
    Helixi272 – 278Combined sources7

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ8U4G1

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini6 – 238PABSUniRule annotationAdd BLAST233

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni51 – 52Polyamine bindingUniRule annotation2
    Regioni142 – 143S-adenosylmethioninamine bindingUniRule annotation2
    Regioni160 – 162Polyamine bindingUniRule annotation3

    Sequence similaritiesi

    Belongs to the spermidine/spermine synthase family.UniRule annotation

    Phylogenomic databases

    eggNOGiarCOG00050 Archaea
    COG0421 LUCA
    HOGENOMiHOG000256146
    KOiK00797
    OMAiLWPGQSF
    OrthoDBiPOG093Z06G4

    Family and domain databases

    Gene3Di2.30.140.10, 1 hit
    HAMAPiMF_00198 Spermidine_synth, 1 hit
    InterProiView protein in InterPro
    IPR030374 PABS
    IPR030373 PABS_CS
    IPR029063 SAM-dependent_MTases
    IPR001045 Spermi_synthase
    IPR035246 Spermidine_synt_N
    IPR037163 Spermidine_synt_N_sf
    PfamiView protein in Pfam
    PF17284 Spermine_synt_N, 1 hit
    SUPFAMiSSF53335 SSF53335, 1 hit
    TIGRFAMsiTIGR00417 speE, 1 hit
    PROSITEiView protein in PROSITE
    PS01330 PABS_1, 1 hit
    PS51006 PABS_2, 1 hit

    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
    PATRICifig|186497.12.peg.132

    Similar proteinsi

    Entry informationi

    Entry nameiSPEE_PYRFU
    AccessioniPrimary (citable) accession number: Q8U4G1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: June 1, 2002
    Last modified: March 28, 2018
    This is version 104 of the entry and version 1 of the sequence. See 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

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