A0A2V1ALB8 · A0A2V1ALB8_9ASCO

  • Protein
    Thiamine thiazole synthase
  • Gene
    THI4
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.

Caution

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

Catalytic activity

Cofactor

Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Note: Binds 1 Fe cation per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site79substrate
Binding site100-101substrate
Binding site108substrate
Binding site173substrate
Binding site210substrate
Binding site225substrate
Binding site282substrate
Binding site292-294substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functioniron ion binding
Molecular Functionpentosyltransferase activity
Biological Processthiamine biosynthetic process
Biological Processthiazole biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Thiamine thiazole synthase
  • Alternative names
    • Thiazole biosynthetic enzyme
      (EC:2.4.2.60
      ) . EC:2.4.2.60 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      THI4
    • ORF names
      CXQ87_000944

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • B09383
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Metschnikowiaceae > Metschnikowiaceae incertae sedis > Candida/Metschnikowiaceae

Accessions

  • Primary accession
    A0A2V1ALB8

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue2082,3-didehydroalanine (Cys)

Post-translational modification

During the catalytic reaction, a sulfide is transferred from Cys-208 to a reaction intermediate, generating a dehydroalanine residue.

Interaction

Subunit

Homooctamer.

Family & Domains

Sequence similarities

Belongs to the THI4 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    331
  • Mass (Da)
    35,573
  • Last updated
    2018-09-12 v1
  • Checksum
    53BC6BEAA77D42B8
MSPPTMVQKPVGSVGNLKTPVVRLDSGANDAQVSFADWEKFNFAPIRESTVSRAMTKRYFNDLDKYTESDIIIVGAGSAGLSAAYVLAKNRPNLKIAIIEASVSPGGGCWLGGQLFSAMVMRKPANLFLDELEIAYEDEGDYVVVKHAALFMSTLMSKVLQFPNVKLFNATAVEDLITRRDESTGELRIAGVVTNWTLVTLNHDTQSCMDPNTLNANVVLSTTGHDGPFGAFSAKRLESLRPKSANEPFELGGMRGLDMNKAEDAIVKGTREVAPGLVIAGMELAEVDGSNRMGPTFGAMALSGVKAAESVLNVVDIRKKQNESCYGGTQN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PKFP01000008
EMBL· GenBank· DDBJ
PVH18033.1
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.
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