D4QF24 · THTA1_STRSQ
- ProteinL-threonine:uridine-5'-aldehyde transaldolase
- GenelipK
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids424 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Transaldolase involved in the biosynthesis of the lipopeptidyl nucleoside antibiotic A-90289 (PubMed:23110675).
Catalyzes the condensation of L-threonine and uridine-5'-aldehyde to form 5'-C-glycyluridine (GlyU) (PubMed:23110675).
Forms (5'S,6'S)-GlyU (PubMed:23110675).
Has no activity with alternative amino acids, such as glycine or serine (PubMed:23110675).
Catalyzes the condensation of L-threonine and uridine-5'-aldehyde to form 5'-C-glycyluridine (GlyU) (PubMed:23110675).
Forms (5'S,6'S)-GlyU (PubMed:23110675).
Has no activity with alternative amino acids, such as glycine or serine (PubMed:23110675).
Catalytic activity
- L-threonine + uridine-5'-aldehyde = (5'S,6'S)-C-glycyluridine + acetaldehydeThis reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
29.2 mM | uridine-5'-aldehyde |
kcat is 40 min-1 with uridine-5'-aldehyde as substrate.
pH Dependence
Optimum pH is 7.5.
Pathway
Antibiotic biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | cobalt ion binding | |
Molecular Function | glycine hydroxymethyltransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | serine binding | |
Molecular Function | zinc ion binding | |
Biological Process | antibiotic biosynthetic process | |
Biological Process | folic acid metabolic process | |
Biological Process | glycine biosynthetic process from serine | |
Biological Process | L-serine catabolic process | |
Biological Process | one-carbon metabolic process | |
Biological Process | tetrahydrofolate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-threonine:uridine-5'-aldehyde transaldolase
- EC number
- Short namesL-Thr:UA transaldolase ; L-Thr:uridine-5'-aldehyde transaldolase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionD4QF24
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 235 | Loss of activity. Cannot bind pyridoxal phosphate. | ||||
Sequence: K → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000459783 | 1-424 | L-threonine:uridine-5'-aldehyde transaldolase | |||
Sequence: MTVGAGGKTSADADPLMLVRAIADADRRAAHALNLVPSENRISPLASLPLASDFYNRYFFNTDGDPLFWEFRGGEDIAHIEALGAAALRRMASARYCNVRPISGMSAMILTVAALSPPGSTVVSVDQNSGGHYATPALLGRLGRRSRLLNCKDGEVDESELAEVLAPGDVALVYVDVQNCVRVPDFRRMSDVIREVSPGTRLYVDASHYLGLVLGGLLANPLDCGADAFGGSTHKSFPGPHKGVIFTNAEDVDESLRSAQFDLVSSHHFAETLALSLAALEVEDRMGDYARATNDNARRLAGALADAGFRVYGDSATGYTDTHQVWVELDGVAAAYALSNRLAEGGIRVNLQSSMPGMSGVHLRLGSNEVTFEGAGPQAIEELAGALVTARERALGPRTVHEIRGRFGAPFYTDPEKLKVEAGL | ||||||
Modified residue | 235 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Structure
Sequence
- Sequence statusComplete
- Length424
- Mass (Da)45,141
- Last updated2010-06-15 v1
- Checksum634040A65B860685