A0A924I295 · A0A924I295_9SPHN

  • Protein
    6,7-dimethyl-8-ribityllumazine synthase
  • Gene
    ribH
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.

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 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site2595-amino-6-(D-ribitylamino)uracil (UniProtKB | ChEBI)
Binding site290-2925-amino-6-(D-ribitylamino)uracil (UniProtKB | ChEBI)
Binding site314-3165-amino-6-(D-ribitylamino)uracil (UniProtKB | ChEBI)
Binding site319-320(2S)-2-hydroxy-3-oxobutyl phosphate (UniProtKB | ChEBI)
Active site322Proton donor
Binding site3465-amino-6-(D-ribitylamino)uracil (UniProtKB | ChEBI)
Binding site360(2S)-2-hydroxy-3-oxobutyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentriboflavin synthase complex
Molecular Function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Molecular Function6,7-dimethyl-8-ribityllumazine synthase activity
Molecular FunctionGTP cyclohydrolase II activity
Molecular Functionmetal ion binding
Biological Processriboflavin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    6,7-dimethyl-8-ribityllumazine synthase
  • EC number
  • Short names
    DMRL synthase
    ; LS
    ; Lumazine synthase

Gene names

    • Name
      ribH
    • ORF names
      H7268_00730

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • FL-bin-363
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingosinicellaceae > Sandarakinorhabdus

Accessions

  • Primary accession
    A0A924I295

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain81-230GTP cyclohydrolase II

Sequence similarities

Belongs to the DMRL synthase family.
In the C-terminal section; belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    387
  • Mass (Da)
    41,025
  • Last updated
    2023-02-22 v1
  • Checksum
    F1771AE9720D0704
PLVARDGGVLVRAGHTEASVDVARLAGLNPSGDICEIMNDDGEMMRLPELIVFARAHGLKIGTIQDLIAYRHAHDRLVKCVAETKITSWHGGEWTAKTYVNTAEYAEHMVLQKGRVEPGKPTLVRVHTMSMFTDLFHEANDRAGQLQRAMDAIGAVGAGIVVIIRDSAPNAISTQMKAKGEGVSVQLRDYGIGAQILVDLGVTDMILLTNAHRTIVGIQGYGLHVVEERPIPGHALSPLPLAGGEKETPLHILIVEARFYSAIADAQLEGARAALEAAGATHDVITVPGALEIPAATAFADGGGQYDGYVALGCVIRGETYHFEVVAGESARAIMALTLDGLPIGNGILTVENEAQAWARARMTEKDKGGEAAKAALAMIALKARFA

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACMPU010000032
EMBL· GenBank· DDBJ
MBC7519610.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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