D4QF24 · THTA1_STRSQ

  • Protein
    L-threonine:uridine-5'-aldehyde transaldolase
  • Gene
    lipK
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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).

Catalytic activity

Cofactor

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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
29.2 mMuridine-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

AspectTerm
Cellular Componentcytoplasm
Molecular Functioncobalt ion binding
Molecular Functionglycine hydroxymethyltransferase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functionserine binding
Molecular Functionzinc ion binding
Biological Processantibiotic biosynthetic process
Biological Processfolic acid metabolic process
Biological Processglycine biosynthetic process from serine
Biological ProcessL-serine catabolic process
Biological Processone-carbon metabolic process
Biological Processtetrahydrofolate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    L-threonine:uridine-5'-aldehyde transaldolase
  • EC number
  • Short names
    L-Thr:UA transaldolase
    ; L-Thr:uridine-5'-aldehyde transaldolase

Gene names

    • Name
      lipK

Organism names

  • Taxonomic identifier
  • Strain
    • SANK 60405
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    D4QF24

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis235Loss of activity. Cannot bind pyridoxal phosphate.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004597831-424L-threonine:uridine-5'-aldehyde transaldolase
Modified residue235N6-(pyridoxal phosphate)lysine

Structure

Family & Domains

Sequence similarities

Belongs to the SHMT family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    424
  • Mass (Da)
    45,141
  • Last updated
    2010-06-15 v1
  • Checksum
    634040A65B860685
MTVGAGGKTSADADPLMLVRAIADADRRAAHALNLVPSENRISPLASLPLASDFYNRYFFNTDGDPLFWEFRGGEDIAHIEALGAAALRRMASARYCNVRPISGMSAMILTVAALSPPGSTVVSVDQNSGGHYATPALLGRLGRRSRLLNCKDGEVDESELAEVLAPGDVALVYVDVQNCVRVPDFRRMSDVIREVSPGTRLYVDASHYLGLVLGGLLANPLDCGADAFGGSTHKSFPGPHKGVIFTNAEDVDESLRSAQFDLVSSHHFAETLALSLAALEVEDRMGDYARATNDNARRLAGALADAGFRVYGDSATGYTDTHQVWVELDGVAAAYALSNRLAEGGIRVNLQSSMPGMSGVHLRLGSNEVTFEGAGPQAIEELAGALVTARERALGPRTVHEIRGRFGAPFYTDPEKLKVEAGL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB530986
EMBL· GenBank· DDBJ
BAJ05887.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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