A0A069Q6I8 · A0A069Q6I8_PSEAI

  • Protein
    Inosine-5'-monophosphate dehydrogenase
  • Gene
    guaB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • 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.

TypeIDPosition(s)Description
Binding site88GDP (UniProtKB | ChEBI)
Binding site98GDP (UniProtKB | ChEBI)
Binding site118GDP (UniProtKB | ChEBI)
Binding site119GDP (UniProtKB | ChEBI)
Binding site120GDP (UniProtKB | ChEBI)
Binding site134ATP (UniProtKB | ChEBI)
Binding site136ATP (UniProtKB | ChEBI)
Binding site137ATP (UniProtKB | ChEBI)
Binding site153ATP (UniProtKB | ChEBI)
Binding site159ATP (UniProtKB | ChEBI)
Binding site180ATP (UniProtKB | ChEBI)
Binding site181ATP (UniProtKB | ChEBI)
Binding site198GDP (UniProtKB | ChEBI)
Binding site199GDP (UniProtKB | ChEBI)
Binding site202GDP (UniProtKB | ChEBI)
Binding site247NAD+ (UniProtKB | ChEBI)
Binding site247-249NAD+ (UniProtKB | ChEBI)
Binding site297-299NAD+ (UniProtKB | ChEBI)
Binding site299K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site301K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site302IMP (UniProtKB | ChEBI)
Active site304Thioimidate intermediate
Binding site304K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site337IMP (UniProtKB | ChEBI)
Binding site337-339IMP (UniProtKB | ChEBI)
Binding site339IMP (UniProtKB | ChEBI)
Binding site360IMP (UniProtKB | ChEBI)
Binding site360-361IMP (UniProtKB | ChEBI)
Binding site361IMP (UniProtKB | ChEBI)
Binding site384IMP (UniProtKB | ChEBI)
Binding site384-388IMP (UniProtKB | ChEBI)
Binding site387IMP (UniProtKB | ChEBI)
Binding site388IMP (UniProtKB | ChEBI)
Active site402Proton acceptor
Binding site417IMP (UniProtKB | ChEBI)
Binding site471K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site472K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site473K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionIMP dehydrogenase activity
Molecular Functionmetal ion 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
      CAZ10_17565
      , CSB93_2499
      , DT376_00630
      , GNQ48_05465
      , GUL26_01290
      , IPC1295_13460
      , IPC737_18950
      , L4V69_09510
      , PAERUG_P19_London_7_VIM_2_05_10_06566

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • P19_London_7_VIM_2_05_10
    • S567_C10_BS
    • CPHL10662
    • PA-W36
    • AR_0356
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A069Q6I8
  • Secondary accessions
    • A0A1S1BUR2

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain93-148CBS
Domain152-210CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    489
  • Mass (Da)
    51,707
  • Last updated
    2014-10-01 v1
  • Checksum
    6D2320AFD52C888B
MLRISQEALTFDDVLLIPGYSEVLPKDVSLKTRLTRGIELNIPLVSAAMDTVTEARLAIAMAQEGGIGIIHKNMGIEQQAAEVRKVKKHETAIVRDPVTVTPSTKIIELLQMAREYGFSGFPVVEQGELVGIVTGRDLRVKPNAGDTVAAIMTPKDKLVTAREGTPLEEMKAKLYENRIEKMLVVDENFYLRGLVTFRDIEKAKTYPLASKDEQGRLRVGAAVGTGADTGERVAALVAAGVDVVVVDTAHGHSKGVIERVRWVKQTFPDVQVIGGNIATAEAAKALAEAGADAVKVGIGPGSICTTRIVAGVGVPQISAIANVAAALEGTGVPLIADGGIRFSGDLAKAMVAGAYCVMMGSMFAGTEEAPGEIELFQGRSYKSYRGMGSLGAMSGSQGSSDRYFQDASAGAEKLVPEGIEGRVPYKGALSAIVHQLMGGLRAAMGYTGSADIQQMRTQPQFVRITGAGMAESHVHDVQITKEAPNYRVG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP027169
EMBL· GenBank· DDBJ
AVK05382.1
EMBL· GenBank· DDBJ
Genomic DNA
CVVU01000267
EMBL· GenBank· DDBJ
CRQ05874.1
EMBL· GenBank· DDBJ
Genomic DNA
WOAD01000003
EMBL· GenBank· DDBJ
MUI34447.1
EMBL· GenBank· DDBJ
Genomic DNA
WXZT01000001
EMBL· GenBank· DDBJ
MZZ10871.1
EMBL· GenBank· DDBJ
Genomic DNA
NFFZ01000008
EMBL· GenBank· DDBJ
OTI60888.1
EMBL· GenBank· DDBJ
Genomic DNA
QORE01000006
EMBL· GenBank· DDBJ
RCI76757.1
EMBL· GenBank· DDBJ
Genomic DNA
NSNE01000007
EMBL· GenBank· DDBJ
RPM16158.1
EMBL· GenBank· DDBJ
Genomic DNA
NSTV01000006
EMBL· GenBank· DDBJ
RPW72278.1
EMBL· GenBank· DDBJ
Genomic DNA
CP136986
EMBL· GenBank· DDBJ
WOS79362.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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