A0A1E4SV00 · A0A1E4SV00_9ASCO

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.

TypeIDPosition(s)Description
Binding site277-279NAD+ (UniProtKB | ChEBI)
Binding site327-329NAD+ (UniProtKB | ChEBI)
Binding site329K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site331K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site332IMP (UniProtKB | ChEBI)
Active site334Thioimidate intermediate
Binding site334K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site367-369IMP (UniProtKB | ChEBI)
Binding site390-391IMP (UniProtKB | ChEBI)
Binding site414-418IMP (UniProtKB | ChEBI)
Active site436Proton acceptor
Binding site448IMP (UniProtKB | ChEBI)
Binding site503K+ (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

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
      CANARDRAFT_238421

Organism names

  • Taxonomic identifier
  • Strain
    • NRRL YB-2248
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Pichiaceae > Ogataea > Ogataea/Candida clade

Accessions

  • Primary accession
    A0A1E4SV00

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain120-181CBS
Domain183-239CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    522
  • Mass (Da)
    56,018
  • Last updated
    2017-01-18 v1
  • Checksum
    791BE87EEE74C48F
MSFENCSNAIDLLSTYEEKDGLSIQQLLDSKIHGGLTYNDFLVLPGKIDFPASIVDLETHLTKKITLKTPFVSSPMDTVTESNMAIKMALLGGIGIIHHNCTADEQAEMVRKVKKYENGFINDPIVISKEITVGQVKAMGEQFGFTSFPVTETGKVGGKLVGIVTSRDIQFHEDDSSSIAEVMTTDLVTGTAGVSLTDGNEILRKSKKGKLPIVDSEGNLVSMLSRTDLQKNLEFPHASKSFQSKQLLCGAAIGTIESDKERLAKLVAAGLDVVVLDSSQGNSVFQIEMIKYIKKTYPDLEVIGGNVVTREQAAQLIVAGVDGLRIGMGSGSICITQEVMACGRPQGTAVYKVTEFANKFGVPCIADGGVGNIGHITKAIALGASCVMMGGMLAGTSESPGEFFYRDGKRLKTYRGMGSIDAMQKTDSNANASTSRYFSEGDKVLVAQGVSGSVLDKGSIVKFIPYLYNGLQHSCQDIGVKSLTELKSSVMAGGVRFELRTPSSQLEGGVHNLYSYEKRLHN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV453865
EMBL· GenBank· DDBJ
ODV83319.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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