A0A7C9HDL8 · A0A7C9HDL8_9BACT

  • Protein
    Biosynthetic arginine decarboxylase
  • Gene
    speA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the biosynthesis of agmatine from arginine.

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

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 site499Proton 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
    • ORF names
      F0475_00670

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • A2879
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Prevotellaceae > Prevotella

Accessions

  • Primary accession
    A0A7C9HDL8

Proteomes

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue99N6-(pyridoxal phosphate)lysine

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain79-342Orn/DAP/Arg decarboxylase 2 N-terminal
Domain368-445Arginine decarboxylase helical bundle
Domain576-629Arginine decarboxylase C-terminal helical

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    630
  • Mass (Da)
    71,364
  • Last updated
    2021-02-10 v1
  • Checksum
    3E6957DC24EDE91A
MKKWTIEDSTELYNTSGWGTSYFGINNKGDVYVTPCKDNTQIDLRDVMDELALRDVTPPVLLRFPDILDNRIEKTSSCFEKAKKEYDFKAENFIIYPIKVNQMQPVVEEIISHGRKFNLGLEAGSKPELHAVIAVQCQSDSLIICNGYKDQSYIELALLAQKMGKRIFIVVEKLNEIDLIARAAKKLNVKPNLGIRIKLASSGSGKWAESGGDASKFGLTSSELLQALETLDAKGLHDSLRLIHFHIGSQITKIRRIQTALNEAAQYYVNLRKMGYNVDFVDCGGGLGVDYDGTRSSSSESSVNYSIQEYVNDCVYTFVDAANKSDIPHPNIITESGRSLSAHHSVLVIDVLETASLPEMSEEFEAKETDHQLVKDLYDIWDNLDARNMLEDWHDAEQIREEALELFSHGLVDLRTRAEIEAMYWSVCHEINNLAKNMKHVPDELRNMDKLLADKYFCNFSLFQSLPDSWAIDQLFPVMPIQRLNERPSRNATLQDITCDSDGKISNFVAMGRSSHVLPVHPLKSNEPYYLGVFLVGAYQEILGDMHNLFGDTNAVHISVKDGGYHIDQIFDGETVEEVLEYVQYNPKKLVRQLEIWVTKSVKQGKISLEEGKEFLSNYRSGLYGYTYLE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VVIQ01000001
EMBL· GenBank· DDBJ
MUL26864.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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