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C3YPU5 · C3YPU5_BRAFL

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.

Type
IDPosition(s)Description
Binding site398-400NAD+ (UniProtKB | ChEBI)
Binding site448-450NAD+ (UniProtKB | ChEBI)
Binding site450K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site452K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site453IMP (UniProtKB | ChEBI)
Active site455Thioimidate intermediate
Binding site455K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site488-490IMP (UniProtKB | ChEBI)
Binding site511-512IMP (UniProtKB | ChEBI)
Binding site535-539IMP (UniProtKB | ChEBI)
Active site553Proton acceptor

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
      BRAFLDRAFT_121137

Organism names

Accessions

  • Primary accession
    C3YPU5

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region67-91Disordered
Compositional bias72-91Basic and acidic residues
Domain238-299CBS
Domain303-361CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    556
  • Mass (Da)
    60,260
  • Last updated
    2009-07-28 v1
  • MD5 Checksum
    D3418A3AB3A0B0CDAB53B046A78841A7
MLQTAVGGWVARACKRYHRPIKERAVPPRVEAGKGYATSMQNARGRGHESVGKRCNDSMIQAGCKQERMAQAADMNRSDSERSTEDPTVTMTEEDSRCMADYLISGGTGYVPDDGMTASQLFGTGEGLTYNDFLILPGFIDFTAEEVRVATNAPSILASIESPCTPNCPVHTEDLTSAMTKKIQLKAPLVSSPMDTVSESDMAIAMALTGGIGIIHSNCTPEFQANEVRKVKKYEQGFIMDPIVLSPEHTVGDVCEMKRKHGFSGIPITENGKLGGKLLGIVTSRDIDFMNSDHHHIKLRDVMTPFEELVVGHAGVSLKEANETLQRSKKGKLPIVNENDELVSLIARTDLKKNRDYPLASKDSKKQLLCGAAIGTREEDKYRVELLVQAGVDLVVLDSSQGNSIYQINMIRYLKQKYSELQVIGGNVVTAAQAKNLIDAGVDGLRVGMGSGSICITQEVMAVGRPQGTAVYKVAEYARRFGVPVIADGGISTVGHITKALALGASTVMMGSLLAGTSEAPGEYFFQDGVRLKKYRGMGSLEAMEKGKASQNRYFR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias72-91Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GG666538
EMBL· GenBank· DDBJ
EEN57879.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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