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A0A1A8WGC9 · A0A1A8WGC9_PLAOA

  • 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 site243-245NAD+ (UniProtKB | ChEBI)
Binding site293-295NAD+ (UniProtKB | ChEBI)
Binding site295K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site297K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site298IMP (UniProtKB | ChEBI)
Active site300Thioimidate intermediate
Binding site300K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site333-335IMP (UniProtKB | ChEBI)
Binding site356-357IMP (UniProtKB | ChEBI)
Binding site380-384IMP (UniProtKB | ChEBI)
Active site399Proton acceptor
Binding site421IMP (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
      POVCU1_012970
      , POVCU2_0071520

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Plasmodium)

Accessions

  • Primary accession
    A0A1A8WGC9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain150-206CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    496
  • Mass (Da)
    54,871
  • Last updated
    2016-10-05 v1
  • MD5 Checksum
    DBB2C7195B5AE174E0D5340A4E01BEFD
MSYTYDDIICMPGYIDFPLSEIDLSNNLTDTICMKTPIISSPMDTVTEHKMSISLALCGGLGIIHNNMSIENQIEEVKKVKRFENGFIFDPYTFSPEHTVADVLATKNKVGYKSYPITVDGKVGSKLAGIITGVDYLYLTDKSKKIKDIMTTDVVTGNYPINLSDANKVLCEEKKSVLPIVNNNYELIALVCRNDMHKNRIFPHASKSQNKQLIVGASISTREHDLERANQLIKNMIDIICIDSSQGNSIYQLDTIKKIKTSYPDIPIIGGNVVTCDQAKNLIDAGADVLRIGMGSGSICTTQDVCAVGRAQGTAVYHVSNYAHTRNIKTIADGGIKNSGNIVKALSLGADFVMLGNLLAATEESCSDYYFENNVRLKIYRGMGSMEAMYNKGFNSKGRYLVEEKRNDNSFEQSEEIKVSQGVSASLVDKGSVLNLIPHLVKAVIHGFQSMGIRNIPELHNRLYSGDLKFDVRSFNTIKEGRISDNLIFSNKKFTQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FLQV01000240
EMBL· GenBank· DDBJ
SBS85786.1
EMBL· GenBank· DDBJ
Genomic DNA
FLQU01001204
EMBL· GenBank· DDBJ
SBS92017.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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