A0A0N0PEW2 · A0A0N0PEW2_PAPXU

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 site267-269NAD+ (UniProtKB | ChEBI)
Binding site317-319NAD+ (UniProtKB | ChEBI)
Binding site319K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site321K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site322IMP (UniProtKB | ChEBI)
Active site324Thioimidate intermediate
Binding site324K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site357-359IMP (UniProtKB | ChEBI)
Binding site380-381IMP (UniProtKB | ChEBI)
Binding site404-408IMP (UniProtKB | ChEBI)
Active site425Proton acceptor
Binding site438IMP (UniProtKB | ChEBI)
Binding site493K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

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

    • Name
      LOC106123538
    • ORF names
      RR46_00233

Organism names

  • Taxonomic identifier
  • Strain
    • Ya'a_city_454_Px
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Lepidoptera > Glossata > Ditrysia > Papilionoidea > Papilionidae > Papilioninae > Papilio

Accessions

  • Primary accession
    A0A0N0PEW2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain108-168CBS
Domain172-230CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    511
  • Mass (Da)
    55,485
  • Last updated
    2015-12-09 v1
  • Checksum
    976C9BE7DFEEBBDA
MMNAEGDLRDGLSAKEIFANSEGLTYNDFLLLPGFINFTAEEVDLTSPLTKKINLKSPLVSTPMDTVTEADMAIAMALCGGIGIIHHNCTPEYQANEVHKVKKYKHGFIRDPVCMGPENTVADVLEAKKKNGFTGYPITENGKLGGRLIGIVTSRDIDFREGDPQLSLKEVMTPIDEMITAQSGVTLQDANYILEKSKKGKLPIINGSGELVALIARTDLKKARSYPNASKDSNKQLLVGAAIGTREADRERLKLLVSNGVDVIVLDSSQGNSTYQIDMIKYIKSNYPNIQVIGGNVVTRMQAKNLIEAGVDALRVGMGSGSICITQEVMACGCPQATAVYQVSSYARQFNVPVIADGGIQSVGHIVKSLALGASTVMMGSLLAGTSEAPGEYFFSDGVRLKKYRGMGSLEAMENKEGKGSAMSRYFHKETDKHRVAQGVSGSIVDKGSVLRFLPYLQTGMQHSCQDLGAPSLTKLREMSYSGDLRFMKRTYSAQLEGNVHGLFSYEKRLF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LADI01003404
EMBL· GenBank· DDBJ
KPJ20584.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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