A0A6L6UBQ0 · A0A6L6UBQ0_9FLAO

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 site251NAD+ (UniProtKB | ChEBI)
Binding site251-253NAD+ (UniProtKB | ChEBI)
Binding site301-303NAD+ (UniProtKB | ChEBI)
Binding site303K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site305K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site306IMP (UniProtKB | ChEBI)
Active site308Thioimidate intermediate
Binding site308K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site341-343IMP (UniProtKB | ChEBI)
Binding site364-365IMP (UniProtKB | ChEBI)
Binding site388-392IMP (UniProtKB | ChEBI)
Active site404Proton acceptor
Binding site419IMP (UniProtKB | ChEBI)
Binding site473K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site474K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site475K+ (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
      GN138_15160

Organism names

  • Taxonomic identifier
  • Strain
    • HL2-2
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Winogradskyella

Accessions

  • Primary accession
    A0A6L6UBQ0

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain97-153CBS
Domain157-217CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    490
  • Mass (Da)
    52,272
  • Last updated
    2020-10-07 v1
  • Checksum
    2D194FE23FA54569
MTAHENKILGEGLTYDDVLLVPAFSEVLPREVNIQSKFTKNITINVPIISAAMDTVTESKMAIAMAQEGGIGVLHKNMTIEQQADKVRRVKRAESGMIIDPVTLPLTATVFDAKSNMAEHSIGGIPIVDENGKLTGIVTNRDLRFEHENAKPIVEVMTKENLVTAAVGTSLKDAEKILQQNKIEKLLIVDDNFILKGLITFRDITKVTQKPNANKDSYGRLRVAAAIGVTGDAVERASALVNAGVDAVIIDTAHGHTKGVVMVLKEIKKKFPKLDVIVGNIATGEAAKYLVEAGADAVKVGIGPGSICTTRVVAGVGFPQFSAVLEVAAAIKGTGVPVIADGGIRYTGDIPKAIAAGADTVMLGSLLAGTKESPGETIIYEGRKFKSYRGMGSVEAMKQGSKDRYFQDVEDDIKKLVPEGIVGRVPYKGELVESIHQFVGGLRAGMGYCGAKDVATLKENGRFVKITSSGINESHPHDVTITKEAPNYSR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WOWS01000008
EMBL· GenBank· DDBJ
MUU79785.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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