E2BHJ7 · E2BHJ7_HARSA

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 site279-281NAD+ (UniProtKB | ChEBI)
Binding site329-331NAD+ (UniProtKB | ChEBI)
Binding site331K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site333K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site334IMP (UniProtKB | ChEBI)
Active site336Thioimidate intermediate
Binding site336K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site369-371IMP (UniProtKB | ChEBI)
Binding site392-393IMP (UniProtKB | ChEBI)
Binding site416-420IMP (UniProtKB | ChEBI)
Active site437Proton 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
      EAI_10308

Organism names

  • Taxonomic identifier
  • Strain
    • R22 G/1
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Formicoidea > Formicidae > Ponerinae > Ponerini > Harpegnathos

Accessions

  • Primary accession
    E2BHJ7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain117-179CBS
Domain184-242CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    523
  • Mass (Da)
    56,754
  • Last updated
    2010-11-30 v1
  • Checksum
    BA784AF4A84FE6C1
MADYVLGNVKASDVPLPDDGTSAERLFASGDGLTYNDFIILPGYIDFTAEEVDLLSPLTKKIMLKAPLVSSPMDTVTESDMAIAMALSGGIGIIHHNCTPEYQANEVHKVKKYKHGFIRDPVVLAPHHMVNDVLNVKAEHGFSGVPVTDTGKVGGKLLGIVTSRDIDFLECLQNYQHKSLSSIMTTLENLITAPAGVTLQEANAILEKSKKGKLPIVNERGELVSLMARTDLKKNRNYPNASKDENKQLLVGAAIGTRSADKQRLHLLEAAGVDVIVLDSSQGNSMYQIEMIRYIKSQYPDLQVIAGNVVTTMQAKNLIEAGADALRVGMGSGSICITQEVMAVGRPQATAVYKVSEYARKFGIPVIADGGIQSVGHIIKALSLGASTVMMGSLLAGTSEAPGEYFFSDGVRLKKYRGMGSLEAMNRKDAKGSAMDRYFHNEMDKLKVAQGVSGSIVDKGSVLKFLPYLTCGIKHSCQDIGARSLSILRSMMYSGELKFERRTHSAQQEGNVHSLFSYEKRLF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL448301
EMBL· GenBank· DDBJ
EFN84850.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp