P60659 · SPEA_SALTY

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 site307-317substrate

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
      STM3086

Organism names

Accessions

  • Primary accession
    P60659
  • Secondary accessions
    • Q8XFQ5

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001499761-658Biosynthetic arginine decarboxylase
Modified residue127N6-(pyridoxal phosphate)lysine

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    658
  • Mass (Da)
    73,833
  • Last updated
    2004-03-29 v1
  • Checksum
    8A689D85DB85D6CF
MSDDMSMGSPSSAGEQGVLRSMQEVAMSSQEASKMLRTYNIAWWGNNYYDVNELGHISVCPDPDVPEARVDLAKLVKAREAQGQRLPALFCFPQILQHRLRSINAAFKRARESYGYNGDYFLVYPIKVNQHRRVIESLIHSGEPLGLEAGSKAELMAVLAHAGMTRSVIVCNGYKDREYIRLALIGEKMGHKVYLVIEKMSEIAIVLEEAERLNVVPRLGVRARLASQGSGKWQSSGGEKSKFGLAATQVLQLVETLRDAGRLDSLQLLHFHLGSQMANIRDIATGVRESARFYVELHKLGVNIQCFDVGGGLGVDYEGTRSQSDCSVNYGLNEYANNIIWAIGDACEEHGLPHPTVITESGRAVTAHHTVLVSNIIGVERNEYTDPTAPAEDAPRALQNLWETWQEMHKPGTRRSLREWLHDSQMDLHDIHIGYSSGAFSLQERAWAEQLYLSMCHEVQKQLDPQNRAHRPIIDELQERMADKMYVNFSLFQSMPDAWGIDQLFPVLPLEGLDQVPERRAVLLDITCDSDGAIDHYIDGDGIATTMPMPEYDPENPPMLGFFMVGAYQEILGNMHNLFGDTEAVDVFVFPDGSVEVELSDEGDTVADMLQYVQLDPKTLLTHFRDQVKQTDLDDALQQQFLEEFEAGLYGYTYLEDE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE006468
EMBL· GenBank· DDBJ
AAL21961.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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