A0A4P6PH60 · A0A4P6PH60_9BACT

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 site257NAD+ (UniProtKB | ChEBI)
Binding site257-259NAD+ (UniProtKB | ChEBI)
Binding site307-309NAD+ (UniProtKB | ChEBI)
Binding site309K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site311K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site312IMP (UniProtKB | ChEBI)
Active site314Thioimidate intermediate
Binding site314K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site346-348IMP (UniProtKB | ChEBI)
Binding site369-370IMP (UniProtKB | ChEBI)
Binding site393-397IMP (UniProtKB | ChEBI)
Active site411Proton acceptor
Binding site423IMP (UniProtKB | ChEBI)
Binding site477K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site479K+ (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
      EGM51_06960

Organism names

Accessions

  • Primary accession
    A0A4P6PH60

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain103-161CBS
Domain165-220CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    494
  • Mass (Da)
    53,360
  • Last updated
    2019-07-31 v1
  • Checksum
    06E01CD57005A461
MSQNQYIQDFMNTFKYEGLTFDDVSLITQYADFLPGDTDISSKLTRNVSVKIPFLSAAMDTVTESRMANSMAMLGGIGVIHKNLEPEVQAQQVSRVKHHLNGLIADPITFSTNDTLETIAERRSEKGYSFNGFPIIDNDGKLAGILTSKDIRFARSKRAAVTEIMTKNVITAPPDTNLKQAYEIMQEHKIGKLPLVNKGKLIALYSYADVRRLIENEEPLFNRDEKYRLRVAAGIGPGDYERAEILNEREVDVLVVDTAHGHTKGVIDMVSWVKNKFPHIDVIGGNIATGEAALALRDAGADAVKVGIGPGSICTTRVVAGVGVPQISAIYAAASALKGEIPVVADGGIRNSGDIAKALVAGADTVMMGSVLAGTEESPGEKIIYEGRQFVIYRGMGSLDAMKSREGSRQRYGLSDDDDIVPQGIEGMVPFAGTVSKVMKQYCGGLQASLGYCGARNIEALKATGKFVRVSSAGAVEAHAHDIKITKEAPNYRR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036201
EMBL· GenBank· DDBJ
QBG47149.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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