A0A5Z1WQN2 · A0A5Z1WQN2_CAMJU

  • 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.

Type
IDPosition(s)Description
Binding site244NAD+ (UniProtKB | ChEBI)
Binding site244-246NAD+ (UniProtKB | ChEBI)
Binding site294-296NAD+ (UniProtKB | ChEBI)
Binding site296K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site298K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site299IMP (UniProtKB | ChEBI)
Active site301Thioimidate intermediate
Binding site301K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site334-336IMP (UniProtKB | ChEBI)
Binding site357-358IMP (UniProtKB | ChEBI)
Binding site381-385IMP (UniProtKB | ChEBI)
Active site397Proton acceptor
Binding site411IMP (UniProtKB | ChEBI)
Binding site465K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site466K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site467K+ (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
    • ORF names
      A0K99_00585
      , BEC39_00840
      , BG250_04290
      , D1228_00585
      , DSN79_01960
      , DYW28_00100
      , E0Z27_00280
      , E8P16_01200
      , F1P90_00140
      , FCT93_01045
      , FKJ47_00285
      , FQW99_00350
      , FRQ07_00960
      , FRQ18_00300
      , FRR83_01070
      , FZW03_00590
      , GC762_03440
      , GNO00_02115
      , YO79_00585

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 137111
    • 260090
    • 724562
    • 735620
    • 766744
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Campylobacteraceae > Campylobacter

Accessions

  • Primary accession
    A0A5Z1WQN2

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain92-149CBS
Domain152-209CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    485
  • Mass (Da)
    52,194
  • Last updated
    2020-04-22 v1
  • Checksum
    B9D4BD368A2B20C2
MKIVKRALTFEDVLLRPGYSEVLPKEVKIHTKLTKNITLNMPLISAAMDTVTEHRAAIMMARLGGLGVIHKNMDIASQVREVKRVKKSESGVIIDPIFVSPKASVAEALEIMAEYRISGVPVVDEDKKLIGILTNRDLRFESDFSNLVENVMTKMPLITAPKGCTLDDAEKIFSTNKVEKLPIVDEQGRLEGLITIKDLKKRKEYPNANKDNFGRLRVGAAIGVGQMDRVDALVEAGVDVVVLDSAHGHSKGIIDTIKAIKTKYPNLDLIAGNIATAAAAKALCEAGVDAVKVGIGPGSICTTRIVSGVGVPQISAIDECVEEANKFGVPVIADGGIKYSGDIAKALAVGASSVMIGSLLAGTDESPGELFTYQGRQYKSYRGMGSLGAMQKGSSDRYFQQGTAQDKLVPEGIEGRVPYVGSIRSVVHQLLGGLRSSMGYVGAKDIEDFQKRAEFVEITTAGLKESHVHDVTITHEAPNYKVNHQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AACAAG010000001
EMBL· GenBank· DDBJ
EAJ7052998.1
EMBL· GenBank· DDBJ
Genomic DNA
AACBBH010000002
EMBL· GenBank· DDBJ
EAJ8288713.1
EMBL· GenBank· DDBJ
Genomic DNA
AACBZE010000001
EMBL· GenBank· DDBJ
EAJ8963728.1
EMBL· GenBank· DDBJ
Genomic DNA
AACCII010000001
EMBL· GenBank· DDBJ
EAJ9718072.1
EMBL· GenBank· DDBJ
Genomic DNA
AACKOK010000001
EMBL· GenBank· DDBJ
EAL0023837.1
EMBL· GenBank· DDBJ
Genomic DNA
AACKPS010000007
EMBL· GenBank· DDBJ
EAL0078570.1
EMBL· GenBank· DDBJ
Genomic DNA
AACPOI010000005
EMBL· GenBank· DDBJ
EAL5936304.1
EMBL· GenBank· DDBJ
Genomic DNA
AACSEO010000001
EMBL· GenBank· DDBJ
EAL8964025.1
EMBL· GenBank· DDBJ
Genomic DNA
AACTES010000001
EMBL· GenBank· DDBJ
EAM0223075.1
EMBL· GenBank· DDBJ
Genomic DNA
AAJBAM010000001
EMBL· GenBank· DDBJ
ECK2339877.1
EMBL· GenBank· DDBJ
Genomic DNA
AAJDCU010000001
EMBL· GenBank· DDBJ
ECK7581147.1
EMBL· GenBank· DDBJ
Genomic DNA
AAJDDU010000002
EMBL· GenBank· DDBJ
ECK7680289.1
EMBL· GenBank· DDBJ
Genomic DNA
AAJDKN010000002
EMBL· GenBank· DDBJ
ECK7960625.1
EMBL· GenBank· DDBJ
Genomic DNA
AAJERN010000001
EMBL· GenBank· DDBJ
ECL0461301.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKCAK010000001
EMBL· GenBank· DDBJ
ECQ6520850.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKFTH010000001
EMBL· GenBank· DDBJ
ECR3388453.1
EMBL· GenBank· DDBJ
Genomic DNA
AAMHGK010000015
EMBL· GenBank· DDBJ
EDH3326223.1
EMBL· GenBank· DDBJ
Genomic DNA
AANOAG010000002
EMBL· GenBank· DDBJ
EDP7180372.1
EMBL· GenBank· DDBJ
Genomic DNA
MKBD01000001
EMBL· GenBank· DDBJ
OEY03961.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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