A0AA35XEV1 · A0AA35XEV1_GEOBA

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 site190-192NAD+ (UniProtKB | ChEBI)
Binding site240-242NAD+ (UniProtKB | ChEBI)
Binding site242K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site244K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site245IMP (UniProtKB | ChEBI)
Active site247Thioimidate intermediate
Binding site247K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site280-282IMP (UniProtKB | ChEBI)
Binding site303-304IMP (UniProtKB | ChEBI)
Binding site327-331IMP (UniProtKB | ChEBI)
Active site344Proton acceptor
Binding site356IMP (UniProtKB | ChEBI)
Binding site411K+ (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
      GBAR_LOCUS30616

Organism names

Accessions

  • Primary accession
    A0AA35XEV1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain30-91CBS
Domain95-153CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    429
  • Mass (Da)
    46,389
  • Last updated
    2024-01-24 v1
  • MD5 Checksum
    23C5B819455847A70CE9BA1309F7351F
MGGIGIIHHNCDVEPQANEVRKVKKYKQGFIMDPVCMSPQNTLNDLVNLKKKSGFSGIPITDTGKMGGVLKGIVTSRDVDFLEDDSLSRPLSDLMTPREDLVVAHYGCTLEEAHQILQTNKKGKLPIVNEKDELIALIARTDLKKSRNFPLASKEDKNQLLVGASVSTFATERERLEALVGAGLDVVVLDSSQGNSIFLIDMVKYIKEKYPDLEVIGGNVVTAQQAKNLIDAGVDALRVGMGSGSICITQEVLAVGRPQGTAVYKVAEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAGTSEAPGQYFFQDGVRLKKYRGMGSLVAMESDGSQQRYFSQSTSVKVAQGVSGSVVDKGSIYLYIPYLYSGLQHSCQDVGARSLTNLRSMMYSGELRFEKRTGSAIVEGGVHGLHSYEKRLF

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0AA35U020A0AA35U020_GEOBAGBAR_LOCUS30616474
A0AA35TX97A0AA35TX97_GEOBAGBAR_LOCUS30616243
A0AA35U039A0AA35U039_GEOBAGBAR_LOCUS30616521
A0AA35XG45A0AA35XG45_GEOBAGBAR_LOCUS30616228

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CASHTH010004335
EMBL· GenBank· DDBJ
CAI8056183.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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