A0A8J6RJU5 · A0A8J6RJU5_9CYAN

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribA
  • 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.

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 )

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.

TypeIDPosition(s)Description
Binding site44-45D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site45Mg2+ 1 (UniProtKB | ChEBI)
Binding site45Mg2+ 2 (UniProtKB | ChEBI)
Binding site49D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site148Essential for DHBP synthase activity
Binding site162-166D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site165Mg2+ 2 (UniProtKB | ChEBI)
Binding site186D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site186Essential for DHBP synthase activity
Binding site276-280GTP (UniProtKB | ChEBI)
Binding site281Zn2+ (UniProtKB | ChEBI); catalytic
Binding site292Zn2+ (UniProtKB | ChEBI); catalytic
Binding site294Zn2+ (UniProtKB | ChEBI); catalytic
Binding site297GTP (UniProtKB | ChEBI)
Binding site319-321GTP (UniProtKB | ChEBI)
Binding site341GTP (UniProtKB | ChEBI)
Active site353Proton acceptor; for GTP cyclohydrolase activity
Active site355Nucleophile; for GTP cyclohydrolase activity
Binding site376GTP (UniProtKB | ChEBI)
Binding site381GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
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
      ribA
    • Synonyms
      ribBA
    • ORF names
      H6F75_26505

Organism names

  • Taxonomic identifier
  • Strain
    • FACHB-131
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Nodosilineales > Nodosilineaceae > Nodosilinea

Accessions

  • Primary accession
    A0A8J6RJU5

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-223DHBP synthase
Region224-581GTP cyclohydrolase II
Domain230-397GTP 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
    581
  • Mass (Da)
    63,341
  • Last updated
    2022-05-25 v1
  • Checksum
    F7AA030EEC6ED9C9
MPPAPRQSPSDLELPSDFQFDSIESALHDLAAGKSIVVVDDENRENEGDVICAAQFATPDIINFMAVEARGLICLAMTGERLDQLDLPLMVSPSAFEDENEQTAFTVSIDAALSWGVTTGISADDRARTIQVAINPNARPQDLRRPGHIFPLRAKEGGVLKRAGHTEAGVDLARLAGLYPAGVICEIQNPDGSMARLPELVNYAKAFGLKLISIADLIHYRLQHERFVQREAVASMPTQFGDFAIYAYRNLLDGSEHVAMVKGDPATFADQSVMVRVHSECLTGDAFGSLRCDCRMQLQAALKMIDAAGRGVVVYLRQEGRGIGLVNKLKAYSLQDMGLDTVEANEKLGLPVDQRNYGIGAQILNDIGVQKFCLITNNPRKIAGIKGYGLDMVSRVPLIIEATAYNSGYLATKAQKLGHLLVQTYLATVAIHWRSGDLPVQERYQKLEHLRELAHSQGLLLQEEARPVAAALFSQPDLIVNLGLDTLPVAGSEVWYHDCAQPQMNAIATLLDKLAAWPEIDQLAFLISGGSDPFSGLQVGLDRQVFHHDAVPTPETVKPSDLCGSLESQRIYVFSSHLLAD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACJOF010000040
EMBL· GenBank· DDBJ
MBD1877041.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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