A0QI09 · RIBBA_MYCA1

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.
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 site28-29D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site29Mg2+ 1 (UniProtKB | ChEBI)
Binding site29Mg2+ 2 (UniProtKB | ChEBI)
Binding site33D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site127Essential for DHBP synthase activity
Binding site141-145D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site144Mg2+ 2 (UniProtKB | ChEBI)
Binding site165D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site165Essential for DHBP synthase activity
Binding site259-263GTP (UniProtKB | ChEBI)
Binding site264Zn2+ (UniProtKB | ChEBI); catalytic
Binding site275Zn2+ (UniProtKB | ChEBI); catalytic
Binding site277Zn2+ (UniProtKB | ChEBI); catalytic
Binding site280GTP (UniProtKB | ChEBI)
Binding site303-305GTP (UniProtKB | ChEBI)
Binding site325GTP (UniProtKB | ChEBI)
Active site337Proton acceptor; for GTP cyclohydrolase activity
Active site339Nucleophile; for GTP cyclohydrolase activity
Binding site360GTP (UniProtKB | ChEBI)
Binding site365GTP (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
    • Ordered locus names
      MAV_3365

Organism names

  • Taxonomic identifier
  • Strain
    • 104
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)

Accessions

  • Primary accession
    A0QI09

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000674231-425Riboflavin biosynthesis protein RibBA

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-204DHBP synthase
Region205-425GTP cyclohydrolase II

Sequence similarities

In the N-terminal section; belongs to the DHBP synthase family.
In the C-terminal section; belongs to the GTP cyclohydrolase II family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    425
  • Mass (Da)
    46,285
  • Last updated
    2007-01-09 v1
  • Checksum
    35C961620A713A35
MTRLDSVERAVADIAAGKAVIVIDDEDRENEGDLIFAAEKATPEMVAFMVRYTSGYLCVPLDGAICDRLGLLPMYAVNQDKHGTAYTVTVDARNGVGTGISASDRATTMRLLADPTSIAEDFTRPGHVVPLRAKDGGVLRRPGHTEAAVDLARMAGLQPAGAICEIVSQKDEGSMAQTDELRVFADEHDLAMITIADLIEWRRKHEKHIERIAEARIPTRHGEFRAIGYTSIYEEVEHVALVRGEIAGPNSDGDDVLVRVHSECLTGDVFGSRRCDCGPQLDAAMAMVAREGRGIVLYMRGHEGRGIGLMHKLQAYQLQDAGEDTVDANLKLGFPADARDYGIGAQILVDLGVRSMRLLTNNPAKRVGLDGYGLHIIERVPLPVRANAENIRYLMTKRDKMGHDLAGLDDFHESVHLPGEFGGAL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000479
EMBL· GenBank· DDBJ
ABK67166.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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