Q72I55 · Q72I55_THET2

Function

function

Catalyzes the biosynthesis of agmatine from arginine.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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 active site.

TypeIDPosition(s)Description
Active site502Proton donor

GO annotations

AspectTerm
Molecular Functionarginine decarboxylase activity
Molecular Functionmetal ion binding
Biological Processarginine catabolic process
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
      TT_C1277

Organism names

Accessions

  • Primary accession
    Q72I55

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue103N6-(pyridoxal phosphate)lysine

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain91-345Orn/DAP/Arg decarboxylase 2 N-terminal
Domain371-452Arginine decarboxylase helical bundle
Domain580-628Arginine decarboxylase C-terminal helical

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    630
  • Mass (Da)
    70,394
  • Last updated
    2004-07-05 v1
  • Checksum
    D80DB3AC026ED8B8
MKVAKRFTLKDAEELYLVPHWSGGFFRVGEKGDLEVTPLGPKGPAASLLEIVEALRDEGRPLPLVLRFPQILEARVRALNEAFLEAMAKYGYQGTYRGVYPVKVNQRRLVLETVARAGRPYHLGLEAGSKPELALILAQDLSEEALITTNGFKDDDFVRLALMGRKLGRNVVITLEKFAELFRVLRLSKELGVKPLLGIRYKLKAKGAGQWEASGGENAKFGLTTPEIVRAVEVLQEEGLLDALVMLHAHIGSQVTDIRRIKAAVREAAQTYVQLRKLGAPLRYLNLGGGLAVDYDGSKTNFYASANYTLSEYAENLVYVTKEVVEAQGEPHPILVTESGRAITAYHEVLVLQVIDVIAPPGEARPSPPPPEAHPLVKELWESLQSLSPKNFQEVYHDAFADKETLQTLYDLGLVSLRDRALAEEIFYHIARRVQAIAQNLPYVPDELEDLEKLLADKLVCNFSVFQSLPDAWAIHQLFPVVPLSRLLEPPTRRATLVDISCDSDGKMDRFIDLHDVRQTLPVHPVRPGEPYYLGVFLVGAYQDVLGSNHNLFGQVGEAHVRVEEEGFAIERFVGGETAERVIEKMGFTARELMLGVERLVRRSRLSPAEKGAFLERYARELQGYTYLED

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017221
EMBL· GenBank· DDBJ
AAS81619.1
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.
FeedbackHelp