E1CG36 · CAP15_STRSQ

  • Protein
    5'-C-glycyluridine monooxygenase-decarboxylase
  • Gene
    cap15
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Monooxygenase-decarboxylase involved in the biosynthesis of the capuramycin-type nucleoside antibiotic A-503083 (PubMed:29343643).
Catalyzes the oxidative decarboxylation of 5'-C-glycyluridine (GlyU) to uridine-5'-carboxamide (CarU) (PubMed:29343643).
Is stereospecific for the (5'S,6'R)-diastereomer of GlyU (PubMed:29343643).
Directly incorporates a single oxygen atom from O2 into the product CarU (PubMed:29343643).

Catalytic activity

Cofactor

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

Note: Requires pyridoxal phosphate as an oxygenase cofactor.

Activity regulation

Activity is dependent on phosphate.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
560 μM(5'S,6'R)-C-glycyluridine
kcat is 0.93 min-1 with (5'S,6'R)-C-glycyluridine as substrate.

pH Dependence

Optimum pH is 7.5.

Pathway

Antibiotic biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site179phosphate (UniProtKB | ChEBI)
Binding site318phosphate (UniProtKB | ChEBI)
Binding site322phosphate (UniProtKB | ChEBI)
Binding site353phosphate (UniProtKB | ChEBI)
Binding site367phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmonooxygenase activity
Biological Processantibiotic biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5'-C-glycyluridine monooxygenase-decarboxylase
  • EC number
  • Alternative names
    • PLP-dependent (5'S,6'R)-GlyU:O2 monooxygenase-decarboxylase

Gene names

    • Name
      cap15
    • Synonyms
      ORF15

Organism names

  • Taxonomic identifier
  • Strain
    • SANK 62799
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    E1CG36

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis23020-fold decrease in specific activity.
Mutagenesis262Loss of activity.
Mutagenesis265Loss of activity.
Mutagenesis303No change in activity.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004597851-3995'-C-glycyluridine monooxygenase-decarboxylase
Modified residue230N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homooctamer; tetramer of homodimers.

Family & Domains

Sequence similarities

Belongs to the SelA family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    399
  • Mass (Da)
    42,004
  • Last updated
    2010-11-30 v1
  • Checksum
    1B0921E4B93D9AF0
MNELEFHPHADRRTGSHTMEYQHLGVVPVVSAQANSTPLGGCTLSDGVIRAMGDAARFHVDMEQLWQAAGSFLAEATGSEDACPVTGAAAGMAIAVAACVAGTDGLRVQRLPDPGDQPNEIVLQKGHSISYGGAPLAQMIALGGGRAVEVGAVNETPRSHVASAVTRRTAALVYVTSRTHAVHRKGVPLDELVAIGREHGVPVIVDAAGEGGLRRWVASGADLVIYSGPKMLGAPTSGFICGRGDLVAACRAQYSGIARPMKVGKENLLGLLQAVREYTAVPEEQRAAEQLERMTKLAARLDKIPGLSARTAQDDSGRTIYRVLLTVDPAAAGRSAATLAEEMRAGIPSIYLRDFKLHLGQLEVDPRALSPDGEESVVRRLEELLLDHGGAPTGMEDAR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB538860
EMBL· GenBank· DDBJ
BAJ19050.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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