Q1PUU5 · Q1PUU5_KUEST

  • Protein
    Inosine-5'-monophosphate dehydrogenase
  • Gene
    guaB
  • 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.

TypeIDPosition(s)Description
Binding site265-267NAD+ (UniProtKB | ChEBI)
Binding site315-317NAD+ (UniProtKB | ChEBI)
Binding site317K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site319K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site320IMP (UniProtKB | ChEBI)
Active site322Thioimidate intermediate
Binding site322K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site356-358IMP (UniProtKB | ChEBI)
Binding site379-380IMP (UniProtKB | ChEBI)
Binding site403-407IMP (UniProtKB | ChEBI)
Active site419Proton acceptor
Binding site431IMP (UniProtKB | ChEBI)
Binding site486K+ (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
      guaB
    • ORF names
      kustb0249

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Bacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Brocadiaceae > Candidatus Kuenenia

Accessions

  • Primary accession
    Q1PUU5

Subcellular Location

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain109-170CBS
Domain172-228CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    511
  • Mass (Da)
    55,648
  • Last updated
    2006-05-16 v1
  • Checksum
    5BF725F084FD7457
MEVNNTPMPPNGLDAKTLFEGGEGITYNDFILLPGHIDFILDTISLDTNLTRNIKIKRPLVSSPMDTVTESRMAISMALLGGIGIIHYNNTIEDQAKEVRKVKRFENGFITDPVVLSPFHTIMDVDTIKDTYGFSGIPITEDGTLNSKLVGIVTKRDIDFEDNRTKPLSEVMTRQLVTASSGISLSDGNKILKESKKGKLPLIDKQGRLVSLMSRTDLLKNEDFPFSSKDKGKQLLVGAALSTREEDRERLAELATAGVDVVVIDSSQGDTIFQIDMVRYVKKHYPHIDVIGGNVVTAKQCKSLIDAGVDSLRIGMGSGSICITQDTLAVGRAQGSAVYHTAKFSREYANIPVIADGGIAHIGHIVKALSLGASAVMMGGLLAGTTESPGEYFYEGGVRVKKYRGMASHEAMEKGGGKRYLSVEDRIKVAQGVSGTVVDKGSVIHLGQYLMQSLLHSLQELGCKSVHDLHQGLYDGNLRFEMRSPSAQTEGSVHDLYSSKEPHLGLLRRVR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CT573074
EMBL· GenBank· DDBJ
CAJ70994.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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