A0A1X2YUU6 · A0A1X2YUU6_BIFAD

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).

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 site47-514-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site834-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site84Mg2+ (UniProtKB | ChEBI)
Binding site108Mg2+ (UniProtKB | ChEBI)
Binding site1274-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site156-1582-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site1594-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine (UniProtKB | ChEBI)
Binding site1952-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site215-2162-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate (UniProtKB | ChEBI)
Binding site476substrate
Binding site505substrate
Binding site534substrate
Binding site570substrate
Binding site590-592substrate
Binding site631-634substrate
Binding site670substrate
Binding site674Zn2+ (UniProtKB | ChEBI)
Binding site697substrate
Binding site738Zn2+ (UniProtKB | ChEBI)
Binding site818[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site821[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site826[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
      thiE
    • Synonyms
      thiC
    • ORF names
      B0070_1320
      , BIFAD42_05920
      , C8077_07100
      , DWX79_05915
      , PL948_00465

Organism names

  • Taxonomic identifier
  • Strains
    • 70B
    • 1-11
    • AF21-27
    • 4-2
    • D31st1_A9_D31t1_170403
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A1X2YUU6

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain18-218Thiamine phosphate synthase/TenI

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    874
  • Mass (Da)
    96,811
  • Last updated
    2017-07-05 v1
  • Checksum
    D4AE71B6880DEA57
MNNYPFASMRDCFDMSAYFVVGPQDCKGRPVTDVVDDALRGGATFIQLRAKDADAKDITEMARDIAQIIEDNGKSDSVAFVIDDRTDVVWQARNKGIKVDGVHIGQTDMEPREARALLGEDAIVGLSAETESLVKLINELPNGCIDYIGAGPLHVSTTKPEASVGGNDGSGHTLDEEQINTICTASEFPVVVGGGVKADDMEMLARSKAAGWFVVSAIAGADDPENATREMVTRWKAVRGDKKHGYAPRVKAAVEETEKPAETGEKKFTNAKEAKAASKLAKQQRVDIAARDSKQRDKAHIRKTTPIHFENEHGSYDLQVPYTEIKLSDTPGVGPNAPFKDYNTEGPKCDPKEGLAPLRLDWILDRGDVEEYEGRRRNLEDDGKRAIKRGKASKEWRGRQHKPMRAKDHPVTQMWYARHNIITPEMRYVAEREHCDVELVRSELAAGRAVMPCNINHPEAEPMIIGSKFLTKLNANMGNSAVTSSIDEEVEKLTWATKWGADTVMDLSTGNDIHTTREWILRNSPVPIGTVPMYQALEKVEDDASKLSWELFRDTVIEQCEQGVDYMTIHAGVLLRFVPLTANRMTGIVSRGGSIMAEWCLQHHQESFLYTHFDELCEIFAKYDVAFSLGDGLRPGSLADANDAAQFAELMTLGELTQRAWKHDVQVMIEGPGHIPFDTVRMNIEMEKAICKDAPFYTLGPLTTDTAPGYDHITSAIGGVEIARYGTAMLCYVTPKEHLGLPNKDDVKQGVIAYKIACHAADIAKHHPHAIDRDNAMSKARFEFRWLDQFNLSYDPDTAIAFHDDTLPAEPAKMAHFCSMCGPKFCSMAISQNIRKKFGNAEAQEKLVADAQTIAAGMRAMSEKFREGGSTLYQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP028341
EMBL· GenBank· DDBJ
AVT45687.1
EMBL· GenBank· DDBJ
Genomic DNA
BPPZ01000002
EMBL· GenBank· DDBJ
GJD13608.1
EMBL· GenBank· DDBJ
Genomic DNA
JAQKOL010000001
EMBL· GenBank· DDBJ
MDB1502611.1
EMBL· GenBank· DDBJ
Genomic DNA
LNKC01000005
EMBL· GenBank· DDBJ
OSG85924.1
EMBL· GenBank· DDBJ
Genomic DNA
QRVT01000002
EMBL· GenBank· DDBJ
RGS65129.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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