A0A0P7HX70 · A0A0P7HX70_9EURY

  • Protein
    Inosine-5'-monophosphate dehydrogenase
  • Gene
    guaB_6
  • 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.
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 site258NAD+ (UniProtKB | ChEBI)
Binding site258-260NAD+ (UniProtKB | ChEBI)
Binding site306-308NAD+ (UniProtKB | ChEBI)
Binding site308K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site310K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site311IMP (UniProtKB | ChEBI)
Active site313Thioimidate intermediate
Binding site313K+ (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 site409Proton acceptor
Binding site422IMP (UniProtKB | ChEBI)
Binding site476K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site477K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site478K+ (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_6
    • Synonyms
      guaB
    • ORF names
      SY89_02442

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CDK2
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae

Accessions

  • Primary accession
    A0A0P7HX70

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain104-162CBS
Domain167-223CBS
Region472-495Disordered

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    495
  • Mass (Da)
    52,475
  • Last updated
    2016-01-20 v1
  • Checksum
    7546968A81E4B52C
MASNGSEPFSEKLRVPEALTFDDVLLRPMESRVEPDAADVSTRVSTNVELQIPILSAAMDTVTEAEMAIGMAREGGLGVLHRSMDTAEMEAQIAQVKRADELVIRRENVVTAAPEQTVNDVDAMMEHEGVSGAPVVDDEDRVLGIISGTDIRPYLEVGESDEVREAMTDEVVTASEDVSARDALELMYDHKIERVPIVDDEEHLVGLVTMQGILARRENENAARDADGRLRVGAAVGPFEDERAVAADEAGADVLFIDCAHAHNLNVLDSARAITETVDADVVLGNVGTRAAAEAAVDFADGLKVGIGPGSICTTRVVSGAGMPQITAVAEVADVASQHDVPVIADGGIRYSGDAIKAIAAGADAVMLGSYFAGTDEAPGRVITMNGKKYKQYRGMGSVGAMQSGGGERYLKEENDEEYVPEGVEAATPYTGTLASELHQLVGGMQSGMGYVGAESIPEFKERSEFIRVSSAGQTEGHPHDVMITDEAPNYSPNE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LGUC01000001
EMBL· GenBank· DDBJ
KPN31693.1
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