E9EMW6 · E9EMW6_METRA

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.

Type
IDPosition(s)Description
Binding site286-288NAD+ (UniProtKB | ChEBI)
Binding site336-338NAD+ (UniProtKB | ChEBI)
Binding site338K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site340K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site341IMP (UniProtKB | ChEBI)
Active site343Thioimidate intermediate
Binding site343K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site376-378IMP (UniProtKB | ChEBI)
Binding site399-400IMP (UniProtKB | ChEBI)
Binding site424-428IMP (UniProtKB | ChEBI)
Active site454Proton acceptor
Binding site466IMP (UniProtKB | ChEBI)
Binding site521K+ (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

    • ORF names
      MAA_00717

Organism names

Accessions

  • Primary accession
    E9EMW6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain129-188CBS
Domain192-248CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    539
  • Mass (Da)
    57,091
  • Last updated
    2011-04-05 v1
  • Checksum
    237C5762B012DA79
MAALDAFGTGKVLDHTTALDVLKEYKTADGLDIHELMDTTKHGGLTYNDFLLMPGYIGFPASEVTLDSAITKRITLKTPFVSSPMDTVTEHEMAIHMALQGGLGVIHHNCSPDAQADMVRKVKRYENGFILDPVVIGRNTTVGEAKALKEKWGFGGFPVTEDGKLGSKLLGIVTNRDLQFEDETDATVANVMVTDLVTAPNGVTLVEANKILAKSKKGKLPIVDKDFNLVSMISRSDLTKNQHFPLASKLPDSKQLLCAAAIGTRPEDKIRLQKLVEAGLDVVILDSSQGNSMYQIEMIKWCKKEFPGLDVIGGNVVTREQAASLIAAGADGLRIGMGSGSACITQEVMAVGRPQAAAVYSVSSFAARFGVPCIADGGVQNVGHIVKGLALGASTVMMGGLLAGTTESPGTSFVSREGKLVKAYRGMGSIDAMQDKKAGGGGKDSQKSNAGTARYFSEGDSVLVAQGVSGSVAHRGSINKFVPYLAAGLKHSMQDCGMKSLAELHQGAANGTVRFELRTSSAQLEGNVNMEAYEKKLYA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ADNJ02000007
EMBL· GenBank· DDBJ
EFZ03643.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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