A0AAJ2UPW9 · A0AAJ2UPW9_9ACTN

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site255NAD+ (UniProtKB | ChEBI)
Binding site304-306NAD+ (UniProtKB | ChEBI)
Binding site306K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site308K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site309IMP (UniProtKB | ChEBI)
Active site311Thioimidate intermediate
Binding site311K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site344-346IMP (UniProtKB | ChEBI)
Binding site367-368IMP (UniProtKB | ChEBI)
Binding site391-395IMP (UniProtKB | ChEBI)
Active site413Proton acceptor
Binding site428IMP (UniProtKB | ChEBI)
Binding site482K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site483K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site484K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
Molecular Functionoxidoreductase activity

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
      PV367_32550

Organism names

  • Taxonomic identifier
  • Strain
    • ND06-05F
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0AAJ2UPW9

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain101-157CBS
Domain161-221CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    500
  • Mass (Da)
    52,518
  • Last updated
    2024-07-24 v1
  • Checksum
    4AA4ECD751CE25D7
MTANVDGVPGKFATLGLTYDDVLLLPGASEVLPNAVDTSSRISRNVRVNIPLLSAAMDKVTESRMAISMARQGGVGVLHRNLSVEDQVNQVDLVKRSESGMVTDPITVHPDATLGEADALCAKFRISGVPVTDGNKKLLGIVTNRDMAFETDRSRQVREVMTPMPLVTGQVGISGAEAMELLRRHKIEKLPLVDDAGILKGLITVKDFVKAEQYPNAAKDSEGRLIVGAAVGASPEALERAQALAEAGVDFLVVDTSHGHNSNALSWMSKIKSSVHVDVIGGNVATRDGAQALIDAGVDGIKVGVGPGSICTTRVVAGIGVPQVTAIYEASLAARPAGVPLIGDGGLQYSGDIGKALAAGADTVMLGSLLAGCEESPGELQFINGKQFKSYRGMGSLGAMQSRGQGKSYSKDRYFQAEVAADDKLVPEGIEGQVPYRGPLGNVLHQLVGGLRQTMGYVGAATIAEMESKGRFVRITSAGLKESHPHDIQMTVEAPNYSRK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JARAWN010000288
EMBL· GenBank· DDBJ
MDX3134414.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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