A0A7S3L7P8 · A0A7S3L7P8_9STRA

  • Protein
    Inosine-5'-monophosphate dehydrogenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site283-285NAD+ (UniProtKB | ChEBI)
Binding site333-335NAD+ (UniProtKB | ChEBI)
Binding site335K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site337K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site338IMP (UniProtKB | ChEBI)
Active site340Thioimidate intermediate
Binding site340K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site373-375IMP (UniProtKB | ChEBI)
Binding site396-397IMP (UniProtKB | ChEBI)
Binding site420-424IMP (UniProtKB | ChEBI)
Active site436Proton acceptor
Binding site450IMP (UniProtKB | ChEBI)
Binding site505K+ (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
      ACOF00016_LOCUS9554

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CCMP127
  • Taxonomic lineage
    Eukaryota > Sar > Stramenopiles > Ochrophyta > Bacillariophyta > Bacillariophyceae > Bacillariophycidae > Thalassiophysales > Catenulaceae > Amphora

Accessions

  • Primary accession
    A0A7S3L7P8

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain124-183CBS
Domain187-245CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    523
  • Mass (Da)
    56,861
  • Last updated
    2021-06-02 v1
  • Checksum
    BF0FF7065D7C6F78
MNGSTNGFKFEPLDEETLHSGAEGFTPSEIFVRNRACVAYTYDDLIMMPGHIGFGLGEISTASKLTKNITLQTPLVSSPMDTVTEHEMAIMMALQGGIGIIHSNLTPEMQASEVRLVKKYKNGFINDPICFSPNDTAEDVFRMKSKKGFSSFPITEDGKMGGRLLGIISNRDTSFIEDASAKISTFMTPRENLVVAKEGLSLLEANDILKTSKKGKLPVVNENDELVALIARTDLQKNRDYPSASKNKSNKQLLVGAAIGTRPNDKDRAKLLVEAGVDVIVIDSSQGDSIYQWEMVRHLKTAHPEIDVIGGNVVTPSQAWNLIQAGVDGLRVGMGIGSICTTQEVCAVGRAQASAVYHVAKFARKHGVPIIADGGIKSTGHITKALTLGAGCVMMGSMLAGTDESPGEYFYQDGVRLKRYRGMGSLEAMTKGSEKRYVWDDNETSVKVAQGVSGAVQDKGTLRRYIPYLVQGIRHGLQDAGCKSVEEAQEKLYKDQLRFEIRSPSAQAEGGVHGLHSYSKRLY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HBIM01011545
EMBL· GenBank· DDBJ
CAE0412286.1
EMBL· GenBank· DDBJ
Transcribed RNA

Similar Proteins

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