A0A3A8AX10 · A0A3A8AX10_9RHOB

  • Protein
    Inosine-5'-monophosphate dehydrogenase
  • Gene
    guaB
  • 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.

TypeIDPosition(s)Description
Binding site245NAD+ (UniProtKB | ChEBI)
Binding site245-247NAD+ (UniProtKB | ChEBI)
Binding site295-297NAD+ (UniProtKB | ChEBI)
Binding site297K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site299K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site300IMP (UniProtKB | ChEBI)
Active site302Thioimidate intermediate
Binding site302K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site333-335IMP (UniProtKB | ChEBI)
Binding site356-357IMP (UniProtKB | ChEBI)
Binding site380-384IMP (UniProtKB | ChEBI)
Active site396Proton acceptor
Binding site410IMP (UniProtKB | ChEBI)
Binding site464K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site465K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site466K+ (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

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
      D6850_05285

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HN-E21
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Roseovarius

Accessions

  • Primary accession
    A0A3A8AX10

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain91-147CBS
Domain151-211CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    482
  • Mass (Da)
    50,550
  • Last updated
    2018-12-05 v1
  • Checksum
    5D367F821CA645E0
MEIREALTFDDVLLVPAASNVLPNTADTRTRVTKSIALNIPLLSSAMDTVTESRMAICLAQAGGMGVIHRNLDLEAQADEVSRVKRFVSGIVYNPVTLSPEQTLADAQALQERYRVTGFPVVDDTGRVVGIVTNRDMRFATSPETPVRVMMTSDDLAILQEPAELEEAKSLMKARRIEKLLVTDGEGRLTGLLTLKDTEQAVLNPDACKDSLGRLRVAAASTVGDAGYERSQALVDAGADMIVIDTAHGHSEGVAVAVERAKKLSNEVQVVAGNVATAEGVRALIGAGADAVKIGIGPGSICTTRMVAGVGVPQLTAIMDGVKAAGDVPVIADGGIKFSGDFAKAIAAGASCAMVGSMIAGTDESPGEVILYQGRSYKSYRGMGSLGAMARGSADRYFQKDAASDKLVPEGIEGRVPYKGSANNVIHQLVGGLRAAMGYTGCATIDAMRGGCEFVRITNAGLSESHVHDVQITRESPNYRIG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RAPE01000001
EMBL· GenBank· DDBJ
RKF16943.1
EMBL· GenBank· DDBJ
Genomic DNA

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