A0A844IDM1 · A0A844IDM1_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.

Type
IDPosition(s)Description
Binding site36-37D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site37Mg2+ 1 (UniProtKB | ChEBI)
Binding site37Mg2+ 2 (UniProtKB | ChEBI)
Binding site41D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site137Essential for DHBP synthase activity
Binding site151-155D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site154Mg2+ 2 (UniProtKB | ChEBI)
Binding site175D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site175Essential for DHBP synthase activity
Binding site265-269GTP (UniProtKB | ChEBI)
Binding site270Zn2+ (UniProtKB | ChEBI); catalytic
Binding site281Zn2+ (UniProtKB | ChEBI); catalytic
Binding site283Zn2+ (UniProtKB | ChEBI); catalytic
Binding site286GTP (UniProtKB | ChEBI)
Binding site308-310GTP (UniProtKB | ChEBI)
Binding site330GTP (UniProtKB | ChEBI)
Active site342Proton acceptor; for GTP cyclohydrolase activity
Active site344Nucleophile; for GTP cyclohydrolase activity
Binding site365GTP (UniProtKB | ChEBI)
Binding site370GTP (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
      ribA
    • Synonyms
      ribBA
    • ORF names
      FJR37_12210

Organism names

  • Taxonomic identifier
  • Strain
    • UHCC 0183
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Aphanizomenonaceae > Aphanizomenon

Accessions

  • Primary accession
    A0A844IDM1

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-212DHBP synthase
Region213-557GTP cyclohydrolase II
Domain222-386GTP 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
    557
  • Mass (Da)
    62,153
  • Last updated
    2021-09-29 v1
  • Checksum
    14C93D2C9E62348D
MSQSNITQTFKFDSIDAALADLKAGRVIVVVDDENRENEGDLICAAQFATPDMINFMAVEARGLICLAMTGDRLDELDLPLMVSTLTDTNQTAFTVSIDAGPHLGVSTGISAEDRARTIQVALNPGTKPEELRRPGHIFPLRARPGGVLKRAGHTEAAVDLSRLAGLYPAGVICEIQNPDGSMARLNQLVEYAKNHHLKIISIADLISYRLQNDRLIYREIITKLPSQFGQFDIYGYRHTLDNTEHVAIVKGDPANFRDEAVMVRMHSECLTGDALGSLRCDCRMQLQAALKMIENAGQGVVVYLRQEGRGIGLVNKLKAYSLQDMGLDTVEANERLGFPADLRDYGMGAQILMDLGIKKIRLITNNPRKIAGVKGYGLDVVDRVPLLIESNDFNSYYLATKAKKLGHMLLQTYLVTVAIHWQDEPESVTERYERLEKIRYLSKNQHLLLQEEARPLGIALFDQPSLTVHLGFDQANIAESNWYQQKDHPYLQAICQILDEIATLPYIQKMEFLIATGSDPLSNLQVQLDRQTFSDGVLPSSLRDNLQTQHIYSFSK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VILC01000027
EMBL· GenBank· DDBJ
MTJ30450.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help