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A0A2R9BHZ6 · A0A2R9BHZ6_PANPA

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. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.

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.

Type
IDPosition(s)Description
Binding site335-337NAD+ (UniProtKB | ChEBI)
Binding site385-387NAD+ (UniProtKB | ChEBI)
Binding site387K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site389K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site390IMP (UniProtKB | ChEBI)
Active site392Thioimidate intermediate
Binding site392K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site425-427IMP (UniProtKB | ChEBI)
Binding site448-449IMP (UniProtKB | ChEBI)
Binding site472-476IMP (UniProtKB | ChEBI)
Active site490Proton acceptor
Binding site502IMP (UniProtKB | ChEBI)
Binding site557K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionDNA binding
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
      IMPDH1
    • Synonyms
      IMPDH

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pan

Accessions

  • Primary accession
    A0A2R9BHZ6

Proteomes

Subcellular Location

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain175-234CBS
Domain240-298CBS
Region560-604Disordered
Compositional bias562-578Polar residues

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    604
  • Mass (Da)
    64,292
  • Last updated
    2018-06-20 v1
  • MD5 Checksum
    2CD1C932EF493411D02E2DBDBC49222C
TSRNATLPALVGGCRRALCEGLGASPRLDLATHPTTPRSELSSVVLLAGVGVQMDRLRRASMADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDRDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGEQGPHTHSFTKSGCTEDSGGGRGGGGDAPQCPLSGTASLHN

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2R9BH10A0A2R9BH10_PANPAIMPDH1517
A0A2R9BH16A0A2R9BH16_PANPAIMPDH1489
A0A2R9BQM5A0A2R9BQM5_PANPAIMPDH1555
A0A2R9BQL5A0A2R9BQL5_PANPAIMPDH1540

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias562-578Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJFE02016439
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02016440
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02016441
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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