A0A923G3B4 · A0A923G3B4_9PSED

  • Protein
    4-hydroxythreonine-4-phosphate dehydrogenase
  • Gene
    pdxA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).

Miscellaneous

The active site is located at the dimer interface.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Note: Binds 1 divalent metal cation per subunit. Can use ions such as Zn2+, Mg2+ or Co2+.

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site136substrate
Binding site137substrate
Binding site166a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site211a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site266a divalent metal cation (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site274substrate
Binding site283substrate
Binding site292substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4-hydroxythreonine-4-phosphate dehydrogenase activity
Molecular Functioncobalt ion binding
Molecular Functionmagnesium ion binding
Molecular FunctionNAD binding
Molecular Functionzinc ion binding
Biological Processpyridoxal phosphate biosynthetic process
Biological Processpyridoxine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4-hydroxythreonine-4-phosphate dehydrogenase
  • EC number
  • Alternative names
    • 4-(phosphohydroxy)-L-threonine dehydrogenase

Gene names

    • Name
      pdxA
    • ORF names
      HU751_00175

Organism names

  • Taxonomic identifier
  • Strain
    • BW13M1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A923G3B4

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Sequence similarities

Belongs to the PdxA family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    329
  • Mass (Da)
    34,960
  • Last updated
    2023-02-22 v1
  • MD5 Checksum
    82721CDE667642EBF52E4FBCD7093D46
MKPQRFAVTPGEPAGIGPDLCLLLAAEAQPHPLIAITSRDLLAERAAQLGLAVSLLPVTPDSFPSLPAPAGSLYVWDTPLANPVVAGQLDKANAAFVLETLTRAGQGCLDGQFAGMITAPVHKGVINESGIAFSGHTEFLADLTHTAQVVMMLATRGLRVALVTTHLPLRDIADAITGERLERVTRILHADMRDKFGIANPRILVCGLNPHAGEGGHLGREEIDIIEPALQRLRAEGMDLRGPLPADTLFTPKYLEHCDAVLAMYHDQGLPVLKYKGFGAAVNVTLGLPIIRTSVDHGTALDLAGTGRIDTGSLRVALETAYQMAENRP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABWRJ010000001
EMBL· GenBank· DDBJ
MBC3444167.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help