A0A1U9JVJ1 · A0A1U9JVJ1_9HYPH

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 site258NAD+ (UniProtKB | ChEBI)
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 site348-350IMP (UniProtKB | ChEBI)
Binding site371-372IMP (UniProtKB | ChEBI)
Binding site395-399IMP (UniProtKB | ChEBI)
Active site411Proton acceptor
Binding site426IMP (UniProtKB | ChEBI)
Binding site480K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site481K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site482K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
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
      guaB
    • ORF names
      BHV28_11870

Organism names

Accessions

  • Primary accession
    A0A1U9JVJ1

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain98-163CBS
Domain164-221CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    499
  • Mass (Da)
    52,759
  • Last updated
    2017-06-07 v1
  • Checksum
    984C5A8FBE72280E
MAKIIESPTGLLALTFDDVLLQPGHSEVMPGQVELKTRIARDIELNLPLLSAAMDTVTESRLAIAMAQAGGLGVIHRNMTPREQAEEVRQVKKFESGMVVNPVTIGPKATLEEALQVMRANGISGIPVVDKKDGANKPGRLVGILTNRDVRFASNPGQQIHELMTHENLITVRENVEQAEAKRLLHHNRIEKLLVVDEEGRCVGLITVRDIERSRLNPDASKDGQGRLRAAAAVSVGKDGVERAERLLEAGVDMLVIDTAHGHSQRVLDAVKDVRRLAPDTAIMAGNVATAAATKALIDCGADAVKVGIGPGSICTTRIVAGVGVPQLSAIMGAVEAADKAGIPVIADGGIKFSGDFAKALAAGAAAAMAGSLLAGTEESPGEVYLHRGRSFKAYRGMGSVGAMARGSADRYFQAEVRDELKLVPEGIEGQVAYKGPIAAVLHQLAGGLRASMGYVGAKNLKEFRKKATFVRITNAGLHESHTHNVAITRESPNYPGSV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP017315
EMBL· GenBank· DDBJ
AQS41873.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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