Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A371KAV2 · A0A371KAV2_9EURY

  • Protein
    Polyamine aminopropyltransferase
  • Gene
    speE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site331S-methyl-5'-thioadenosine (UniProtKB | ChEBI)
Binding site374spermidine (UniProtKB | ChEBI)
Binding site400spermidine (UniProtKB | ChEBI)
Binding site418S-methyl-5'-thioadenosine (UniProtKB | ChEBI)
Binding site452-453S-methyl-5'-thioadenosine (UniProtKB | ChEBI)
Active site470Proton acceptor

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionspermidine synthase activity
Biological Processspermidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Polyamine aminopropyltransferase
  • Alternative names
    • Putrescine aminopropyltransferase
      (PAPT
      )
    • Spermidine synthase
      (SPDS
      ; SPDSY
      ) (EC:2.5.1.16
      ) . EC:2.5.1.16 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      speE
    • ORF names
      DEQ67_12855

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Atlit-48N
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax

Accessions

  • Primary accession
    A0A371KAV2

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-29Helical
Transmembrane41-62Helical
Transmembrane74-96Helical
Transmembrane108-128Helical
Transmembrane182-201Helical
Transmembrane207-228Helical
Transmembrane274-291Helical

Keywords

Interaction

Subunit

Homodimer or homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain297-556PABS

Sequence similarities

Belongs to the spermidine/spermine synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    608
  • Mass (Da)
    66,692
  • Last updated
    2018-11-07 v1
  • MD5 Checksum
    F5B31E2C2D0ABC49EFAF566838BC60E2
MSNTRTDTATLLTLTFVVSFCSFAYEFVYSELLTVMYGGTVTQYVITVGLYFFSLGIGAALSDDLDGETLGGNFFRTEVLLAAAAPAGFLLIVGLNSVRIPQAVPAELVWTVARLPVVVVGFLSGFELPLLTRMFDDLDGDGSSTPSWLRTVGTRIHDFVVAAVGTLWTVERTEGRRSGLSVVLAMDYVGGLAGAVVYARVLYPGIGLIPTIFVLALLNGVAALVFVAHFGAWSWWPLGGDEASASAGTGGNAAASARTDGSDRSLSAARVSKTLLVVCLLLTATYAGVVAKHDAADERLSQLYLEQQIENEYPPGAIRATVTSQETTAYQHVIRYDRTWTGTGPNPHFDGRTERCLRLGAAVQLCESWADSYHEGLVDVPMSLVDPGPDTKVLVVGGGDWIAVDHLREYGVTVDHVDLDGEFMRDAKTDPFFARWHDDAYEYDRLNTTVADGYRYLQKTNETYDLVLLDIPGATDDDLLTLYSTEFYRSVRTHLSEDGVAVTWGYSPDAYPEHHKAFVNTVGAAGFTRELSYWVREDLDDDGETERVEQFYVLAPGDRPRLTGDGATRYVRAREEHYGAVEWHAVPHYRGVRENSIFHPNYDILVDT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QEQI01000003
EMBL· GenBank· DDBJ
RDZ31083.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help