A0A8J6S9G8 · A0A8J6S9G8_9CYAN

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribA
  • 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 site43-44D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site44Mg2+ 1 (UniProtKB | ChEBI)
Binding site44Mg2+ 2 (UniProtKB | ChEBI)
Binding site48D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site144Essential for DHBP synthase activity
Binding site158-162D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site161Mg2+ 2 (UniProtKB | ChEBI)
Binding site182D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site182Essential for DHBP synthase activity
Binding site272-276GTP (UniProtKB | ChEBI)
Binding site277Zn2+ (UniProtKB | ChEBI); catalytic
Binding site288Zn2+ (UniProtKB | ChEBI); catalytic
Binding site290Zn2+ (UniProtKB | ChEBI); catalytic
Binding site293GTP (UniProtKB | ChEBI)
Binding site315-317GTP (UniProtKB | ChEBI)
Binding site337GTP (UniProtKB | ChEBI)
Active site349Proton acceptor; for GTP cyclohydrolase activity
Active site351Nucleophile; for GTP cyclohydrolase activity
Binding site372GTP (UniProtKB | ChEBI)
Binding site377GTP (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
      ribA
    • Synonyms
      ribBA
    • ORF names
      H6F79_11200

Organism names

  • Taxonomic identifier
  • Strain
    • FACHB-69
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Leptolyngbyales > Trichocoleusaceae > Trichocoleus

Accessions

  • Primary accession
    A0A8J6S9G8

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-219DHBP synthase
Region220-564GTP cyclohydrolase II
Domain229-393GTP 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
    564
  • Mass (Da)
    62,423
  • Last updated
    2022-05-25 v1
  • Checksum
    D44D9359485D6E28
MPQSQDAKHRAASNQTFKFDSIDAALADLKAGRMVVVVDDESRENEGDLICAAQFATPDTINFMAVYARGLICLALTGDRLDELDLPLMVSNNTDSNQTAFTISIDASPTMGVRTGISAEDRALTIQVAINPATSPQDLRRPGHIFPLRAREGGVLKRAGHTEAGVDLPKLAGLYPAGVICEIQNPDGSMARLPELIEYSKMHNLKIISIADLISYRLNHERFVCRETIAELPTQFGNFQIYAYRNTLDQSETVAIVKGNPADFNDKKVMVRMHSECLTGDALGSLRCDCRMQLQAALKMIENAGSGVVVYLRQEGRGIGLINKLKAYSLQDMGLDTVEANERLGFPADLRNYGVGAQILNDLGITKICLITNNPRKIAGLKGYGLEVVDRVPLLIEANDYNSIYLATKAQKLGHMLLQTYLVTVALHWQDEPQVTERYERLDKLRHLARSHDLLLQEETRPVAIALFGKPSLTVHLGFDQPHLAASDWYQDNGHPYVKAIAQILDALLQWQHLEGLEFMISTGLDPLTGLQIHLDRQTFPIGTLPSSVCDNLETQKIYSFQGF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACJOS010000061
EMBL· GenBank· DDBJ
MBD1932372.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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