A0A6A2SE99 · A0A6A2SE99_BIFLN

  • Protein
    Multifunctional fusion protein
  • Gene
    thiC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).

Caution

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

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site48-524-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site844-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site85Mg2+ (UniProtKB | ChEBI)
Binding site109Mg2+ (UniProtKB | ChEBI)
Binding site1284-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site157-1592-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site1604-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site1962-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site216-2172-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site487substrate
Binding site516substrate
Binding site545substrate
Binding site581substrate
Binding site601-603substrate
Binding site642-645substrate
Binding site681substrate
Binding site685Zn2+ (UniProtKB | ChEBI)
Binding site708substrate
Binding site749Zn2+ (UniProtKB | ChEBI)
Binding site829[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site832[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site837[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functioncarbon-carbon lyase activity
Molecular Functionmagnesium ion binding
Molecular Functionthiamine-phosphate diphosphorylase activity
Molecular Functionzinc ion binding
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Phosphomethylpyrimidine synthase
  • EC number
  • Alternative names
    • Hydroxymethylpyrimidine phosphate synthase
    • Thiamine biosynthesis protein ThiC
      (HMP-P synthase
      ; HMP-phosphate synthase
      ; HMPP synthase
      )
  • Recommended name
    Thiamine-phosphate synthase
  • EC number
  • Short names
    TP synthase
    ; TPS
  • Alternative names
    • Thiamine-phosphate pyrophosphorylase
      (TMP pyrophosphorylase
      ; TMP-PPase
      )

Gene names

    • Name
      thiC
    • Synonyms
      thiE
    • ORF names
      GBC97_07255
      , GBK08_07365

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • BIOML-A166
    • BIOML-A320
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A6A2SE99

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain19-219Thiamine phosphate synthase/TenI
Region255-311Disordered
Compositional bias276-293Basic and acidic residues

Sequence similarities

Belongs to the ThiC family.
Belongs to the thiamine-phosphate synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    917
  • Mass (Da)
    100,279
  • Last updated
    2020-06-17 v1
  • Checksum
    36C3F42DEA0183F3
MSNEYPYASMRDSFDLSAYFVVGPEDCKGRPLTDVVDQALHGGATFIQLRAKEADASELTDMARDIAQIIEDNEKSDSVAFVIDDRADVVWQARRKGIKVDGVHIGQTDMEPREARALLGDEAIVGLSAETESLVRLINELPDGCIDYIGAGPLHVSTTKPEASVGGNDGSGKTLDAAQINTICVASEFPVVVGGGVTAADMAMLAGTKAAGWFVVSAIAGAENPEEAARTMVEGWKAVRGDKKHGYAPRVVTHTPATDTQAAQEGAAKPGSEATEKKFTNAKDAKDAQKLAKQQRVDIAARGSKQRDKAHIRKTKSVPFTYQYGSYDLEVPYTEIKLSDTPGVGPNPPFHDYNTEGPKCDPKEGLKPLRLDWIRDRGDIEDYEGRRRNLEDDGKRAIKRGRATKEWRGRKHEPMRAKDHPITQMWYARHGIITPEMQYVATRENCDVELVRSELAAGRAVMPCNINHPEAEPMIIGSAFLTKLNANMGNSAVTSSIDEEVEKLTWATKWGADTVMDLSTGNDIHTTREWILRNSPVPIGTVPMYQALEKVEDDASKLSWELFRDTVIEQCEQGVDYMTIHAGVLLRYVPLTANRVTGIVSRGGSIMADWCLRHHQESFLYTHFDELCDIFAKYDVAFSLGDGLRPGSLADANDAAQLSELMTLGELTERAWAKDVQVMIEGPGHVPFDTVRMNIELEKAVCHNAPFYTLGPLTTDTAPGYDHITSAIGATEIARYGTAMLCYVTPKEHLGLPNKDDVKQGVIAYKIACHAADIAKHHPHAVDRDNAISKARFEFRWLDQFNLSYDPDTAIAFHDDTLPAEPAKMAHFCSMCGPKFCSMAISQNIRKAFGGEAAQQQIVKEAAAGIDSEALATAKANVDNGVVSANVLSPEEILAGMDAMSEKYTAQGGKLYSTAQE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias276-293Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WEAY01000012
EMBL· GenBank· DDBJ
KAB6837613.1
EMBL· GenBank· DDBJ
Genomic DNA
WDVF01000012
EMBL· GenBank· DDBJ
KAB7134656.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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