Q2RST7 · THIC_RHORT

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.

Catalytic activity

Cofactor

[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.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site215substrate
Binding site244substrate
Binding site273substrate
Binding site309substrate
Binding site329-331substrate
Binding site370-373substrate
Binding site409substrate
Binding site413Zn2+ (UniProtKB | ChEBI)
Binding site436substrate
Binding site477Zn2+ (UniProtKB | ChEBI)
Binding site557[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site560[4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site565[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 Functionzinc ion binding
Biological Processthiamine biosynthetic process
Biological Processthiamine diphosphate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphomethylpyrimidine synthase
  • EC number
  • Alternative names
    • Hydroxymethylpyrimidine phosphate synthase
      (HMP-P synthase
      ; HMP-phosphate synthase
      ; HMPP synthase
      )
    • Thiamine biosynthesis protein ThiC

Gene names

    • Name
      thiC
    • Ordered locus names
      Rru_A2008

Organism names

Accessions

  • Primary accession
    Q2RST7

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002422981-621Phosphomethylpyrimidine synthase

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias1-19Polar residues
Region1-29Disordered

Sequence similarities

Belongs to the ThiC family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    621
  • Mass (Da)
    66,602
  • Last updated
    2006-01-24 v1
  • Checksum
    73ED29E7D7D1C7F9
MTAPFLSSLSPTSPLASATAPFPGSRKVYARPADAPHLRVPFREIILSDPGEAPVRVADPSGPYSDPEATIDLRQGLARHRASWASARGNSTVTAGRPAPSEGDFEAFPLTYAPLRRRDETPFTQLEYARAGVITDEMIYVATRENLGRDSAVAGACARLAGGEAFGAALPAHVTPEFVRAEIAAGRAIIPANINHPELEPTIIGRNFLVKVNANIGNSALGSSIEDEVAKLVWAIRWGADTVMDLSTGKAIHATREWILRNSPVPIGTVPLYQALEKVGGDATRLDWAVFEDTLIEQCEQGVDYFTIHAGVRLAHIPLTASRTTGIVSRGGSILAKWCLSHHRENFLYERFADICAILRRYDVAFSLGDGLRPGSVADANDAAQFAELDTLGALTAVAWEHGCQVMVEGPGHVPMHKIKANMDRQLATCGEAPFYTLGPLTTDIAPGHDHITSAIGAAMIGWFGTAMLCYVTPKEHLGLPDRADVKAGVIAYKLAAHAADIAKGHPAAQLRDDAISRARFDFRWSDQFNLGLDPEGARAFHDETLPHAAHKTAHFCSMCGPKFCSMKISHDIRDGALEGADALTQAGLDQMSATFRASGGEVHLDAQALDALAWEGKPAR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-19Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000230
EMBL· GenBank· DDBJ
ABC22808.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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