A0A1V9BW05 · A0A1V9BW05_9BACI

Function

function

Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion.

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site51Zn2+ (UniProtKB | ChEBI); catalytic
Active site53Proton donor
Binding site76Zn2+ (UniProtKB | ChEBI); catalytic
Binding site85Zn2+ (UniProtKB | ChEBI); catalytic
Binding site155NADP+ (UniProtKB | ChEBI)
Binding site169NADP+ (UniProtKB | ChEBI)
Binding site171NADP+ (UniProtKB | ChEBI)
Binding site185substrate
Binding site197NADP+ (UniProtKB | ChEBI)
Binding site201NADP+ (UniProtKB | ChEBI)
Binding site205substrate
Binding site208substrate
Binding site223NADP+ (UniProtKB | ChEBI)
Binding site291substrate
Binding site293-299NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function5-amino-6-(5-phosphoribosylamino)uracil reductase activity
Molecular Functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
Molecular FunctionNADP binding
Molecular Functionzinc ion binding
Biological Processriboflavin biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Riboflavin biosynthesis protein RibD

Including 2 domains:

  • Recommended name
    Diaminohydroxyphosphoribosylaminopyrimidine deaminase
  • EC number
  • Short names
    DRAP deaminase
  • Alternative names
    • Riboflavin-specific deaminase
  • Recommended name
    5-amino-6-(5-phosphoribosylamino)uracil reductase
  • EC number
  • Alternative names
    • HTP reductase

Gene names

    • ORF names
      B9L19_06810

Organism names

  • Taxonomic identifier
  • Strain
    • BGSC 93A1
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Geobacillus > Geobacillus thermoleovorans group

Accessions

  • Primary accession
    A0A1V9BW05

Proteomes

Family & Domains

Sequence similarities

In the C-terminal section; belongs to the HTP reductase family.
In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    380
  • Mass (Da)
    40,710
  • Last updated
    2017-06-07 v1
  • Checksum
    E04428C326E98DF8
MHNDEHYMRLALDVAKAGVGQTSPNPAVGAVVVNGGTVVGLGAHLKAGEPHAEVYAIRMAGEKARGATVYVTLEPCSHYGKTPPCADLLIQAGVRRVVVATTDPNPLVAGKGIAKLRQAGIDVDVGVLKDEADELNRMFFHYIAAKTPFVTLKFACSLDGKIATATGESKWITSSAAREDVHRLRAQHDAILVGVNTVLTDNPKLTVRFGEKRKNPLRIILDTKLRTPLDAHVVADKEAETWIITGGVSREQAAAYERLGVRVFSMPTAQIDVRDVLRLLGEQGVMSLFVEGGSRVHDSFLRAGAVNEVIAYIAPKLIGGRGAPTSVGGLGFARLAEAVELDIRRIETIGPDIKIVAAPKRKEESLCSLALLKRSARSNK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NEWK01000001
EMBL· GenBank· DDBJ
OXB89749.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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