E1CG36 · CAP15_STRSQ
- Protein5'-C-glycyluridine monooxygenase-decarboxylase
- Genecap15
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids399 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- (5'S,6'R)-C-glycyluridine + O2 = CO2 + H2O + uridine-5'-carboxamideThis reaction proceeds in the forward direction.
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 179 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 318 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 322 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 353 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 367 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | monooxygenase activity | |
Biological Process | antibiotic biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5'-C-glycyluridine monooxygenase-decarboxylase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionE1CG36
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 230 | 20-fold decrease in specific activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 262 | Loss of activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 265 | Loss of activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 303 | No change in activity. | ||||
Sequence: K → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000459785 | 1-399 | 5'-C-glycyluridine monooxygenase-decarboxylase | |||
Sequence: MNELEFHPHADRRTGSHTMEYQHLGVVPVVSAQANSTPLGGCTLSDGVIRAMGDAARFHVDMEQLWQAAGSFLAEATGSEDACPVTGAAAGMAIAVAACVAGTDGLRVQRLPDPGDQPNEIVLQKGHSISYGGAPLAQMIALGGGRAVEVGAVNETPRSHVASAVTRRTAALVYVTSRTHAVHRKGVPLDELVAIGREHGVPVIVDAAGEGGLRRWVASGADLVIYSGPKMLGAPTSGFICGRGDLVAACRAQYSGIARPMKVGKENLLGLLQAVREYTAVPEEQRAAEQLERMTKLAARLDKIPGLSARTAQDDSGRTIYRVLLTVDPAAAGRSAATLAEEMRAGIPSIYLRDFKLHLGQLEVDPRALSPDGEESVVRRLEELLLDHGGAPTGMEDAR | ||||||
Modified residue | 230 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homooctamer; tetramer of homodimers.
Structure
Sequence
- Sequence statusComplete
- Length399
- Mass (Da)42,004
- Last updated2010-11-30 v1
- Checksum1B0921E4B93D9AF0
Keywords
- Technical term