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.

Q083L6 · SPEA_SHEFN

Function

function

Catalyzes the biosynthesis of agmatine from arginine.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site286-296substrate

GO annotations

AspectTerm
Molecular Functionarginine decarboxylase activity
Molecular Functionmetal ion binding
Biological Processarginine catabolic process
Biological Processputrescine biosynthetic process from arginine
Biological Processspermidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Biosynthetic arginine decarboxylase
  • EC number
  • Short names
    ADC

Gene names

    • Name
      speA
    • Ordered locus names
      Sfri_1698

Organism names

Accessions

  • Primary accession
    Q083L6

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_10000242681-636Biosynthetic arginine decarboxylase
Modified residue101N6-(pyridoxal phosphate)lysine

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    636
  • Mass (Da)
    71,191
  • Last updated
    2006-10-31 v1
  • MD5 Checksum
    35E3F568A3B074A292F884AF05FFC46B
MSDWSIEDARSGYNVTHWSQGFYGIREDGEVTVSPNPQNPDHKVGLNELAKSMVEAGVSLPVLVRFPQILHHRVESLCEAFNDAIKKYDYQNDYLLVYPIKVNQQKTVVEEILASQKSKEVPQLGLEAGSKPELMAVLAMAQKASSVIVCNGYKDKEYIRLALIGEKLGHKVYIVLEKMSELKMVLIEAEKLGITPRLGLRVRLAFQGKGKWQASGGEKSKFGLSAAQVLKVIAELKSANMLDSLQLLHFHLGSQIANIRDIRQGVSEAGRFYCELRQLGASIDCFDVGGGLAVDYDGTRSQSNNSMNYGLNEYANNIVNVLTDLCNEYEQPMPRIISESGRHLTAHHAVLITDVIGTEAYQPENIQEPSEDAPQLLHNMWQSWLEISGRYDQRAIIEIYHDSQSDISEAHSLFAVGQLSLADRAWAEQANLRVCHEVKGLLSNNNRYHRPVIDELNEKLADKFFVNFSLFQSLPDAWGIDQVFPVLPLSGLDKAPERRAVMLDITCDSDGIVDQYVDGQGIETTLPVPAWSADSPYLIGFFMVGAYQEILGDMHNLFGDTNSAVVRIDERGLSQIESVLEGDTVADVLRYVNLDAVDFMRTYEELVNQHIVEEERASILEELQLGLKGYTYLEDF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000447
EMBL· GenBank· DDBJ
ABI71549.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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