Q5ZV75 · THI5_LEGPH

Function

function

Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway (PubMed:33034117).
Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP) (Probable). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme (By similarity).
The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme (By similarity).

Catalytic activity

Cofactor

Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site70
Binding site118-121pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
Molecular Functionmetal ion binding
Molecular Functionvitamin B6 binding
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
  • EC number
  • Short names
    HMP-P synthase
    ; Hydroxymethylpyrimidine phosphate synthase
  • Alternative names
    • Thiamine biosynthesis protein 5
    • Thiamine pyrimidine synthase

Gene names

    • Name
      thi5
    • Synonyms
      nmt1
      , thi3
    • Ordered locus names
      lpg1565

Organism names

Accessions

  • Primary accession
    Q5ZV75

Proteomes

Phenotypes & Variants

Disruption phenotype

Growth auxotrophic for thiamine; growth partially restored by hydroxymethylpyrimidine (HMP).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis70Decreases pyridoxal phosphate (PLP) binding.
Mutagenesis118Decreases catalytic activity.
Mutagenesis119Decreases catalytic activity.
Mutagenesis120Decreases catalytic activity.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004520851-3164-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
Modified residue66N6-(pyridoxal phosphate)lysine

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif191-195CCCFC; essential for catalytic activity, may be the site of iron coordination

Sequence similarities

Belongs to the NMT1/THI5 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    316
  • Mass (Da)
    35,276
  • Last updated
    2004-11-23 v1
  • Checksum
    07A59B40553DA971
MAMSSLKSRVTLLLNWYTNPYHTPILVAQQLGFYSEEDIKLAILEPADPSDVTEIVGLGTVDFGVKAMIHTVAAKAKGYPVTSIGTLLDEPPTGLIALKSSGINSFQDIVGKRVGYIGEFGKKIIDDLASLAGIDPTSYKTVRIGMNVTDAIYRDVIDTGIGFINFQKVELEHLCGETVFLRIDQLAGLGCCCFCSIQFIVPEITLQQPELVKGFLRATQRGAAYTTEKPEEAYELLCQAKPQLRTPLYQKIFTRTLPFFSRTLINVDRDWDKVGRYTKHLKIIDEHFDISQCYTNRFLPDTPYSDLKPIACCLEN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE017354
EMBL· GenBank· DDBJ
AAU27647.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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