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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)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.
    OMAiRSYHEPL.
    OrthoDBiPOG093Z06G4.

    Family and domain databases

    HAMAPiMF_00198. Spermidine_synth. 1 hit.
    InterProiView protein in InterPro
    IPR030374. PABS.
    IPR030373. PABS_CS.
    IPR029063. SAM-dependent_MTases.
    IPR001045. Spermi_synthase.
    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.

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1MJFX-ray1.80A/B1-281[»]
    ProteinModelPortaliQ8U4G1.
    SMRiQ8U4G1.
    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.
    OrthoDBiPOG093Z06G4.

    Enzyme and pathway databases

    UniPathwayiUPA00248; UER00314.
    BRENDAi2.5.1.104. 5243.
    SABIO-RKiQ8U4G1.

    Miscellaneous databases

    EvolutionaryTraceiQ8U4G1.

    Family and domain databases

    HAMAPiMF_00198. Spermidine_synth. 1 hit.
    InterProiView protein in InterPro
    IPR030374. PABS.
    IPR030373. PABS_CS.
    IPR029063. SAM-dependent_MTases.
    IPR001045. Spermi_synthase.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    TIGRFAMsiTIGR00417. speE. 1 hit.
    PROSITEiView protein in PROSITE
    PS01330. PABS_1. 1 hit.
    PS51006. PABS_2. 1 hit.
    ProtoNetiSearch...

    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: May 10, 2017
    This is version 100 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

    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.