A0A7K0ENI4 · A0A7K0ENI4_9BACT

  • 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 site36-37D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site37Mg2+ 1 (UniProtKB | ChEBI)
Binding site37Mg2+ 2 (UniProtKB | ChEBI)
Binding site41D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site136Essential for DHBP synthase activity
Binding site150-154D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site153Mg2+ 2 (UniProtKB | ChEBI)
Binding site174D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site174Essential for DHBP synthase activity
Binding site262-266GTP (UniProtKB | ChEBI)
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Binding site278Zn2+ (UniProtKB | ChEBI); catalytic
Binding site280Zn2+ (UniProtKB | ChEBI); catalytic
Binding site283GTP (UniProtKB | ChEBI)
Binding site305-307GTP (UniProtKB | ChEBI)
Binding site327GTP (UniProtKB | ChEBI)
Active site339Proton acceptor; for GTP cyclohydrolase activity
Active site341Nucleophile; for GTP cyclohydrolase activity
Binding site362GTP (UniProtKB | ChEBI)
Binding site367GTP (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
      GJJ30_19030

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KCTC 52001
  • Taxonomic lineage
    Bacteria > Bacteroidota > Cytophagia > Cytophagales > Spirosomataceae > Larkinella

Accessions

  • Primary accession
    A0A7K0ENI4

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-211DHBP synthase
Region212-415GTP cyclohydrolase II
Domain221-383GTP 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
    415
  • Mass (Da)
    45,685
  • Last updated
    2021-04-07 v1
  • Checksum
    BBADA6AB50912421
MSNNNTNPGSLLDRIEDAVQDIRDGKIIIVVDDEDRENEGDMICAAEKITPEMVNFMIKEGRGLMCAPLTDARCQELGLEMMVGNNTSVHTTPFTVSVDLLGNGCTTGISASDRAKTIRALVDPETKPEDLGRPGHIFPLRAVDGGVIRRAGHTEAAIDFARLAGLQPAGVLIEVLNEDGTMARLPQLREMADKFGMKLVSIQDLIGYRLQQESLIKREIGVNMPTGYGDFELIAYKQLNTDDTHLALIKGTWEKNEPVLVRVHSSCVTGDIFGSCRCDCGEQLHASMKMVEAEGKGVVLYMFQEGRGIGLMNKLKAYKLQEMGRDTVEANLELGLPMDARDYGVGAQILRDLGITKLRLITNNPKKRAGLMGYGLEIVETVPIDIRPNPHNEVYLRTKRDKMGHELSHVSDPTV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WJXZ01000012
EMBL· GenBank· DDBJ
MRS63403.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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