A0A154BT93 · A0A154BT93_ANASB

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 site27-28D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site28Mg2+ 1 (UniProtKB | ChEBI)
Binding site28Mg2+ 2 (UniProtKB | ChEBI)
Binding site32D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site125Essential for DHBP synthase activity
Binding site139-143D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site142Mg2+ 2 (UniProtKB | ChEBI)
Binding site163D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site163Essential for DHBP synthase activity
Binding site251-255GTP (UniProtKB | ChEBI)
Binding site256Zn2+ (UniProtKB | ChEBI); catalytic
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Binding site272GTP (UniProtKB | ChEBI)
Binding site294-296GTP (UniProtKB | ChEBI)
Binding site316GTP (UniProtKB | ChEBI)
Active site328Proton acceptor; for GTP cyclohydrolase activity
Active site330Nucleophile; for GTP cyclohydrolase activity
Binding site351GTP (UniProtKB | ChEBI)
Binding site356GTP (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
      AXX12_03420

Organism names

  • Taxonomic identifier
  • Strain
    • RU4
  • Taxonomic lineage
    Bacteria > Bacillota > Negativicutes > Selenomonadales > Sporomusaceae > Anaerosporomusa

Accessions

  • Primary accession
    A0A154BT93

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-200DHBP synthase
Region201-404GTP cyclohydrolase II
Domain207-372GTP 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
    404
  • Mass (Da)
    44,164
  • Last updated
    2016-06-08 v1
  • Checksum
    4F834DEE85332A7D
MKFSTIEEAIRDIREGRMVVVVDDEDRENEGDLLMAAEKVTPEAVNFMAINGRGLICMPVAGSRLDELGIGPMVCENTEALCTAFTVSIDAKSVTTGISAHERAATIQAVLDPCTNPEDLRRPGHIFPLRYREGGVLRRAGHTEAAVDLARLAGLYPAGVICEVMNDDGTMARVPQLVEFTTKHNLSLISIADLIKYRTFHEKLVQRTAAASMPTKYGTFEVFAYESPLDNLCHLALVKGDVKGEPNVLVRVHSECLTGDVLGSLRCDCGEQLALALKRIEEEGKGVLLYMRQEGRGIGLANKIKAYALQDKGKDTVEANVILGFPADLRDYGIGAQILADLGLTSIRLLTNNPKKRAGLEGYGLTITERLPIEVKSNKFNKRYLSVKRAKLGHLLKTTEEGLS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LSGP01000013
EMBL· GenBank· DDBJ
KYZ77196.1
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.
FeedbackHelp