Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A014MHQ3 · A0A014MHQ3_9BURK

Function

function

Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

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

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site153-amino-2-oxopropyl phosphate (UniProtKB | ChEBI)
Binding site263-amino-2-oxopropyl phosphate (UniProtKB | ChEBI)
Active site51Proton acceptor
Binding site531-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Binding site581-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Active site82Proton acceptor
Binding site1121-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI)
Site163Transition state stabilizer
Active site203Proton donor
Binding site2043-amino-2-oxopropyl phosphate (UniProtKB | ChEBI)
Binding site226-2273-amino-2-oxopropyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionpyridoxine 5'-phosphate synthase activity
Biological Processpyridoxine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyridoxine 5'-phosphate synthase
  • EC number
  • Short names
    PNP synthase

Gene names

    • Name
      pdxJ
    • ORF names
      AX13_10605

Organism names

  • Taxonomic identifier
  • Strain
    • DA1877
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Comamonas

Accessions

  • Primary accession
    A0A014MHQ3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homooctamer; tetramer of dimers.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the PNP synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    257
  • Mass (Da)
    27,576
  • Last updated
    2014-06-11 v1
  • MD5 Checksum
    5ED5B8A24566494D57A339F1EF2BCDA4
MTASTPSRRTALSVNVNKVALVRNTRHLGIPSVTRAAQLCLAAGAQGITIHPRPDERHIRGTDVFELAALMRDWPQAEFNIEGNPTQNLMAFIREVRPHQATFVPDSEDQFTSDHGWNFPQDAERLAPLIAECRALGVRVSLFMDPVPAQMAAAQAVGADRVELYTEPYAAAWGTAEQNAQLALYAQAAQAALDAGLEVNAGHDLNRDNLAAFVSQVPGLAEVSIGHALIADALELGYAATVTAYQACIDAGMAQRP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JBOK01000003
EMBL· GenBank· DDBJ
EXU81246.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help