A0A978TZG7 · A0A978TZG7_9CYAN

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 site91-92D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site92Mg2+ 1 (UniProtKB | ChEBI)
Binding site92Mg2+ 2 (UniProtKB | ChEBI)
Binding site96D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site193Essential for DHBP synthase activity
Binding site207-211D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site210Mg2+ 2 (UniProtKB | ChEBI)
Binding site231D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site231Essential for DHBP synthase activity
Binding site321-325GTP (UniProtKB | ChEBI)
Binding site326Zn2+ (UniProtKB | ChEBI); catalytic
Binding site337Zn2+ (UniProtKB | ChEBI); catalytic
Binding site339Zn2+ (UniProtKB | ChEBI); catalytic
Binding site342GTP (UniProtKB | ChEBI)
Binding site364-366GTP (UniProtKB | ChEBI)
Binding site386GTP (UniProtKB | ChEBI)
Active site398Proton acceptor; for GTP cyclohydrolase activity
Active site400Nucleophile; for GTP cyclohydrolase activity
Binding site421GTP (UniProtKB | ChEBI)
Binding site426GTP (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

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
      IGS37_05420

Organism names

Accessions

  • Primary accession
    A0A978TZG7

Proteomes

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-64Disordered
Region1-268DHBP synthase
Compositional bias33-64Polar residues
Region269-625GTP cyclohydrolase II
Domain276-442GTP 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
    625
  • Mass (Da)
    68,969
  • Last updated
    2023-02-22 v1
  • Checksum
    ACF9096DB8A61ABE
MATRPRPRLTELGSCNIDDKITPPHPSHPPPKIKSSLQKTSHLIQDSSVEPLHRQDPSSSTSPTFAFDSIESALADLKAGRAVVVVDDENRENEGDLICAAQFATPDMINFMAVEARGLICLAMTGDRLDQLELPLMVSNTTDDSEQTAFTVSIDGAVHLGVSTGISAEDRARTIQIAINPASKPSDLRRPGHIFPLRAKEGGVLKRAGHTEAGVDLARLAGLYPAGVICEIQNPDGSMARLPELIEYAKHHNLKIISIADLISYRLQHERFVRREAVAELPTQFGNFKIYAYRNLLDNSEHVAMVKGDPSTFKERPVMVRVHSECLTGDALGSLRCDCRMQLQAALKMIENAGAGVVVYLRQEGRGIGLVNKLKAYSLQDLGLDTVEANQRLGFPADQRNYGMGAQILNDIGVKQFILITNNPRKIAGLKGYGLEMVDRMPLLIEATPYNADYLATKAEKLGHLLLQTYLVTVAIRWQDEPLSVTEKYERLEKLRHLAKLHDLLVQEEARSVAIALFHGSSLIVHLGLSQPEAVAANWYEEPHSAQRKAIGQLLDDLAAWPSVQQLEFLVAAGQDPMTNLRVQLSRQIFRLDHPTLADSPKPSQVCEALETQRIYVFSTHSPDV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias33-64Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DVEB01000097
EMBL· GenBank· DDBJ
HIK54585.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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