A0A329K8P9 · A0A329K8P9_9MYCO

  • 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.

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 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
    • ORF names
      DQP58_23515

Organism names

  • Taxonomic identifier
  • Strain
    • GF76
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)

Accessions

  • Primary accession
    A0A329K8P9

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-204DHBP synthase
Region205-425GTP cyclohydrolase II
Domain211-381GTP 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
    425
  • Mass (Da)
    46,217
  • Last updated
    2018-10-10 v1
  • Checksum
    5EDF6B0124E0415E
MTRLDSVERAVADIAAGKAVIVIDDEDRENEGDLIFAAEKATPEMVAFMVRYTSGYLCVPLDGEICDRLGLLPMYAVNQDKHGTAYTVTVDARRGVGTGISASDRATTMRLLADPTSVADDFTRPGHVVPLRAKDGGVLRRPGHTEAAVDLARLAGLQPAGAICEIVSQKDEGAMAQTEELRVFADEHDLAMITIADLIEWRRKHEKHIARIAEARIPTRHGEFRAIGYASIYEEVEHVALVRGDISGPNSDGDDVLVRVHSECLTGDVFGSRRCDCGPQLDAAMAMVAREGRGIVLYMRGHEGRGIGLMHKLQAYQLQDAGEDTVDANLKLGLPADARDYGIGAQILVDLGVRSMRLLTNNPAKRVGLDGYGLHIIERVPLPVRANAENIRYLMTKRDKMGHDLAGLDDFHESVHLPGEFGGAL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QMEU01000125
EMBL· GenBank· DDBJ
RAU90401.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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