A0A2U4EZA0 · A0A2U4EZA0_9SPIR

Function

function

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site17substrate
Binding site39substrate
Binding site66-75substrate
Active site68Proton donor
Binding site125substrate
Binding site187substrate
Binding site196substrate
Binding site216substrate
Binding site217substrate
Binding site3385-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site3425-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site3445-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site364-3725-phospho-alpha-D-ribose 1-diphosphate (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site368orotate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmagnesium ion binding
Molecular Functionorotate phosphoribosyltransferase activity
Molecular Functionorotidine-5'-phosphate decarboxylase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Process'de novo' UMP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Orotidine 5'-phosphate decarboxylase
  • EC number
  • Alternative names
    • OMP decarboxylase
      (OMPDCase
      ; OMPdecase
      )
  • Recommended name
    Orotate phosphoribosyltransferase
  • EC number
  • Short names
    OPRT
    ; OPRTase

Gene names

    • Name
      pyrF
    • Synonyms
      pyrE
    • ORF names
      A966_08034

Organism names

  • Taxonomic identifier
  • Strain
    • 30446
  • Taxonomic lineage
    Bacteria > Spirochaetota > Spirochaetia > Brachyspirales > Brachyspiraceae > Brachyspira

Accessions

  • Primary accession
    A0A2U4EZA0

Proteomes

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-232Orotidine 5'-phosphate decarboxylase

Sequence similarities

Belongs to the OMP decarboxylase family. Type 1 subfamily.
In the C-terminal section; belongs to the OMP decarboxylase family.
In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    451
  • Mass (Da)
    50,132
  • Last updated
    2018-07-18 v1
  • Checksum
    B862C049DBC67C59
MTKLSENPKERLIIALDFNSMGEAAKLIDELGDEAVFYKVGLELFLYTKGEIIEYLAGKNKKVFLDLKFHDIPNTTAMASLFAAKQNVFMFNVHTSGGKKMMEKTVEEIKKLNKDNLIIGVTILTSLSENDVKNMFSSNLALTDLAVNWAKLGKESGLDGVVCSPKEAALIKRECGENFRTICPGVRPKWASTDDQERVMTPKEAIENGCDYLVVGRPITRNEDRVKACKMIVEEIAEGLENNKKAKSKLIASALLNTKAVKLNVKEPFTFVSGIKSPIYCDNRYVIGFPKERKIIVDAFMNILKGKDFDVIAGTATAGIPWASFIAYELNKPLCYIRAEKKEHGRGKQIEGAECSGKKLILIEDLISTGGSSIKAFEAAKAEGAIGLEIIAIFSYEFEKAYKNFEEAGIKFSSLSNFSSLMEIAKDEKYITEEELSKALEWNKNPDSWGK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ALNZ01000026
EMBL· GenBank· DDBJ
EKV56972.1
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