A0A0E3ZXF8 · A0A0E3ZXF8_9BACT

  • 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.

TypeIDPosition(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)
Site150Essential for DHBP synthase activity
Binding site164-168D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site167Mg2+ 2 (UniProtKB | ChEBI)
Binding site188D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site188Essential 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
      ribBA
    • ORF names
      SD10_21435

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DG5A
  • Taxonomic lineage
    Bacteria > Bacteroidota > Cytophagia > Cytophagales > Cytophagaceae > Spirosoma

Accessions

  • Primary accession
    A0A0E3ZXF8

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-225DHBP synthase
Region226-430GTP cyclohydrolase II
Domain235-397GTP 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    47,374
  • Last updated
    2015-06-24 v1
  • Checksum
    D31D3D491B9A15AE
MSNNSTNSETTAQNPGNTIDLNPIRLDRIEDAIADIKAGKIVLVVDDEDRENEGDMICAAEMITPEMVNFMVREARGLMCAPLTQERCDELGLDMMVTSNTSVHTTPFTVSVDLLGNGCTTGISASDRSKTIQALVDPNTTPDDLGRPGHIFPLRAVEGGVIRRAGHTEAAVDLARLAGLSPVGVLIEVLNEDGTMARLPELRVLADRFGMKLVSIQDLIEYRLRTETLIRREIGVDMPTEWGHFDLIAYKQSNTGDTHLALIKGSWEPNEPVLVRVHSSCVTGDIFGSCRCDCGPQLHASMKMVEAEGKGIVVYMFQEGRGIGLINKLKAYKLQEMGRDTVEANLDLGLPMDSRDYGVGAQILRDLGVRKLRLISNNPKKRAGLMGYGLEIVDTVPIEIQPNPHNERYLRTKRDKMGHTIMNEPVNEEQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP010429
EMBL· GenBank· DDBJ
AKD57073.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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