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A0A7T5E690 · A0A7T5E690_9CYAN

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribBA
  • 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 conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.

Catalytic activity

Cofactor

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

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.

Features

Showing features for binding site, site, active site.

Type
IDPosition(s)Description
Binding site50-51D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site51Mg2+ 2 (UniProtKB | ChEBI)
Binding site51Mg2+ 1 (UniProtKB | ChEBI)
Binding site55D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site154Essential for DHBP synthase activity
Binding site168-172D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site171Mg2+ 2 (UniProtKB | ChEBI)
Binding site192D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site192Essential for DHBP synthase activity
Binding site282-286GTP (UniProtKB | ChEBI)
Binding site287Zn2+ (UniProtKB | ChEBI); catalytic
Binding site298Zn2+ (UniProtKB | ChEBI); catalytic
Binding site300Zn2+ (UniProtKB | ChEBI); catalytic
Binding site303GTP (UniProtKB | ChEBI)
Binding site325-327GTP (UniProtKB | ChEBI)
Binding site347GTP (UniProtKB | ChEBI)
Active site359Proton acceptor; for GTP cyclohydrolase activity
Active site361Nucleophile; for GTP cyclohydrolase activity
Binding site382GTP (UniProtKB | ChEBI)
Binding site387GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Molecular FunctionGTP binding
Molecular FunctionGTP cyclohydrolase II activity
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular Functionzinc ion binding
Biological Processriboflavin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Riboflavin biosynthesis protein RibBA

Including 2 domains:

  • Recommended name
    3,4-dihydroxy-2-butanone 4-phosphate synthase
  • EC number
  • Short names
    DHBP synthase
  • Recommended name
    GTP cyclohydrolase-2
  • EC number
  • Alternative names
    • GTP cyclohydrolase II

Gene names

    • Name
      ribBA
    • ORF names
      GFS31_34980

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BL0902
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Leptolyngbyales > Leptolyngbyaceae > Leptolyngbya group > Leptolyngbya

Accessions

  • Primary accession
    A0A7T5E690

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-24Polar residues
Region1-25Disordered
Region1-229DHBP synthase
Region230-584GTP cyclohydrolase II
Domain236-403GTP cyclohydrolase II

Sequence similarities

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
    Complete
  • Length
    584
  • Mass (Da)
    64,264
  • Last updated
    2021-09-29 v1
  • MD5 Checksum
    F18FCD471A11F063D289B1EB2679C7F8
MVNPESGNWSSAAQPSTDASPPDFQFDSIESALQDLAAGKSIVVVDDENRENEGDVICAAQFATPDNINFMAVEARGLICLAMTGERLDELDLPLMVSHSAFEDENEQTAFTVSIDAALSWGVTTGISAEDRARTIQVAINPKAKPSDLRRPGHIFPLRAKEGGVLKRAGHTEAGVDLARLAGLYPAGVICEIQNPDGSMARLPELVDYAKTFGLKLISIADLIRYRLQHERFVQREAVAELPTQFGLFHIYAYRNLLDDSEHVALVKGDPATFDQHSVMVRVHSECLTGDAFGSLRCDCRMQLQAALKMIESAGRGVVVYLRQEGRGIGLVNKLKAYSLQDMGLDTVEANEKLGLPVDQRNYGIGAQILNDIGVKKFCLITNNPRKIAGLKGYGLDMVDRVPLIIEATPYNSNYLSTKAQKLGHLMLQTYLATVAIHWQRGPLSTEDRYEKLEKLRYLAQENGLLLQEEARSVASALFSQPHQIIHLGLESAEAVHPDWYTEASQPQLRAITTILDALATWPDLSQMAFLISNGSDPFNGLQVNLDRQIFHRGDSAADVKPSALADNLETQRIYVFSNHIPSD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-24Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP046155
EMBL· GenBank· DDBJ
QQE66795.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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