B5Z806 · B5Z806_HELPG

Function

function

Catalyzes the biosynthesis of agmatine from arginine.

Cofactor

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

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

Features

Showing features for active site.

161550100150200250300350400450500550600
TypeIDPosition(s)Description
Active site487Proton donor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
    Arginine decarboxylase
  • EC number

Gene names

    • Ordered locus names
      HPG27_951

Organism names

  • Taxonomic identifier
  • Strain
    • G27
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter

Accessions

  • Primary accession
    B5Z806

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue89N6-(pyridoxal phosphate)lysine

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain77-331Orn/DAP/Arg decarboxylase 2 N-terminal
Domain359-431Arginine decarboxylase helical bundle
Domain562-611Arginine 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
    615
  • Mass (Da)
    70,257
  • Last updated
    2008-11-25 v1
  • Checksum
    49A7F60467B8184C
MQEVHDYGINFWSNNEFKIEKGLVKVCHGKNPSLLEIVQSVRDKGYRGPLLVRFPHLVQKQIKSLFDAFSLAIKEYQYSGAFKAVFPLKVNQMPSFVFPLVQGAKGLDYGLEAGSKSELIIAMSYTNPKAPITVNGFKDKEMIELGFIAKSMQHEITLTIEGLNELKTIIAVAKQNDFVACPKIGIRIRLHSAGTGVWAKSGGINSKFGLSSTEVLEAMRLLEENDLLEHFHMIHFHIGSQISDISPLKKALREAGNLYAELRKMGAKNLNSVNIGGGLAVEYTQHKHHQDKNYTLEEFSADVVFLLREIVKNKQEIEPDIFIESGRYISANHAVLVAPVLELFSHEYNEKSLKIKESNNPPLIDEMLDLLANINEKNAIEYLHDSFDHTESLFTLFDLGYIDLIDRSNTEVLAHLIVKKAVQLLYVKDHNDILRIQEQVQERYLLNCSFFQSLPDYWGLRQNFPVMPLNKLDEKPTRSASLWDITCDSDGEIAFDSTKPLFLHDIDIDEEEYFLAFFLVGAYQEVLGMKHNLFTHPTEFSVVFDEKGDYEVEDICEAQTILDVLDDLDYDTKEIERLLKQKIEDNNQLDMEEKKEIMGRLYVMLSENGYLRTIS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001173
EMBL· GenBank· DDBJ
ACI27705.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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