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A0A061DA96 · A0A061DA96_BABBI

  • Protein
    Inosine-5'-monophosphate dehydrogenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

K+ (UniProtKB | Rhea| CHEBI:29103 )

Activity regulation

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site258-260NAD+ (UniProtKB | ChEBI)
Binding site308-310NAD+ (UniProtKB | ChEBI)
Binding site310K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site312K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site313IMP (UniProtKB | ChEBI)
Active site315Thioimidate intermediate
Binding site315K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site350-352IMP (UniProtKB | ChEBI)
Binding site373-374IMP (UniProtKB | ChEBI)
Binding site397-401IMP (UniProtKB | ChEBI)
Active site421Proton acceptor
Binding site433IMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionIMP dehydrogenase activity
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding
Biological ProcessGMP biosynthetic process
Biological ProcessGTP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inosine-5'-monophosphate dehydrogenase
  • EC number
  • Short names
    IMP dehydrogenase
    ; IMPD
    ; IMPDH

Gene names

    • ORF names
      BBBOND_0401280

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Bond
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia

Accessions

  • Primary accession
    A0A061DA96

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain102-161CBS
Domain165-221CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    505
  • Mass (Da)
    54,398
  • Last updated
    2014-09-03 v1
  • MD5 Checksum
    A990388257BB9CF9D6168D6BB11427F3
MADGSSAAEIFDTTTIGYTYDDLILLPDYISGPNTNVNLSTNLTRKIRLSAPVVSSPMDTVTESKMAVEIALQGGIGIIHNNLTQEELIEEVRKVKRFENGFIVDPYVLTPNHTVGDWMAIRDKYGFKSIPITTDGKRDSKLEGIVTSGDVCFVQDKSTKISEVMTRDPIVGKHPLTLQEANTILCDIKKGILPIVNDKGELVSIVSRSDIKKNRKFPIAAKNEHMQLLVGVAISTRAGALERAAKLIEAGADVLVIDSSQGNSVYQIDLIKQLKQANPEIQVIGGNVVTGRQAKNLIDAGVDGLRVGMGCGSICSTQGVCGVGRPQATAVFYVSRYAREYGHGCPVIADGGIRSSGDIMKALALGASCCMLGGAIAGTIESPGDFFYHNGIRVKQYRGMGSKAAFMSARQKTGDRGSIRRYHMEEDQPMVSQGVAGYTSDKGSISTLIPTMLQAVKHGMQNIGCYDIKSLHEGLYSGSVRFEVRSYNALVEGNVSTSLMMQNQS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LK391710
EMBL· GenBank· DDBJ
CDR97636.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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