U9U2A7 · U9U2A7_RHIID

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 site299-301NAD+ (UniProtKB | ChEBI)
Binding site350-352NAD+ (UniProtKB | ChEBI)
Binding site352K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site354K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site355IMP (UniProtKB | ChEBI)
Active site357Thioimidate intermediate
Binding site357K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site390-392IMP (UniProtKB | ChEBI)
Binding site413-414IMP (UniProtKB | ChEBI)
Binding site437-441IMP (UniProtKB | ChEBI)
Active site463Proton acceptor
Binding site475IMP (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
      GLOIN_2v1632275
      , GLOINDRAFT_346493

Organism names

Accessions

  • Primary accession
    U9U2A7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-23Disordered
Domain142-204CBS
Domain205-261CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    549
  • Mass (Da)
    59,184
  • Last updated
    2014-01-22 v1
  • Checksum
    2D86C44B11D16FFF
MVHNETNNGFKANTANSAASNNTTYLDPKQAKNYLKEYSSPDGLSAEEIMNSIVNGGLTYNDFLILPGYIDFPASEVSLESRITRNIVLKTPFMSSPMDTVTETDMAINMALLGGVGVIHCNCSPEEQAEMVRKVKKFENGFITDPVCLTPNHTVADVRRIKAQFGYSGIPITANGKLYSILLGMVTARDIQFHEDDNTLLKDVMTTDLVVAHEGVTLEEANQILRQSKRGKLPIINQRGELVALLARSDLLKNLNFPLASKSAHSKQLICAAAIGTKPDDKLRLKKLVDAGLDIVVLDSSQGNSSFQIEMIKHIKNTYGDSLEVIAGNVVTREQAAALIEAGADALRVGMGSGSICITQEVMAVGRPQGTAVYNVAEFANKFGIPVIADGGIQNVGHITKALALGASAVMMGSLLAGATESPGEYFYHEGQRLKKYRGMGSLDAMERRTPGTSGAPNNAAKRYFSERDVIKVAQGVAGAVIDKGSIRKFVPYLITGLQHGLQDIGARNLATLGENVRSGKIRFELRTAAAQIEGGVHGLYSYEKRLFS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KI282848
EMBL· GenBank· DDBJ
ESA14499.1
EMBL· GenBank· DDBJ
Genomic DNA
AUPC02000146
EMBL· GenBank· DDBJ
POG68831.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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