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A0A1A2P466 · A0A1A2P466_9MYCO

  • 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 site286NAD+ (UniProtKB | ChEBI)
Binding site286-288NAD+ (UniProtKB | ChEBI)
Binding site337-339NAD+ (UniProtKB | ChEBI)
Binding site339K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site341K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site342IMP (UniProtKB | ChEBI)
Active site344Thioimidate intermediate
Binding site344K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site377-379IMP (UniProtKB | ChEBI)
Binding site400-401IMP (UniProtKB | ChEBI)
Binding site424-428IMP (UniProtKB | ChEBI)
Active site450Proton acceptor
Binding site465IMP (UniProtKB | ChEBI)
Binding site518K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site519K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site520K+ (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
      A5693_14605

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • E1319
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium

Accessions

  • Primary accession
    A0A1A2P466

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain132-188CBS
Domain192-249CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    536
  • Mass (Da)
    55,306
  • Last updated
    2016-10-05 v1
  • MD5 Checksum
    1DB108F8BC2B084D12D931DFAFC514BB
MTRGTSHLEDSSDLVGSPYVRDTPVSGFLDEPIATGGDNPHKVAMLGLTFDDVLLLPAASDVVPATADTSSQLTRKIRLKVPLVSSAMDTVTESRMAIAMARAGGMGVLHRNLPVAEQAGQVETVKRSEAGMVTDPVTCRPDNTLAQVDALCARFRISGLPVVDEAGALVGIITNRDMRFEVDQGKKVAEVMTKAPLITAQEGVSADAALGLLRRNKIEKLPVVDGHGRLTGLITVKDFVKTEQHPLATKDSDGRLLVGAAVGVGGDAWVRAMMLVDAGVDVLIVDTAHAHNRLVLDMVGKLKAEVGEKVEVIGGNVATRSAAAALVAAGADAVKVGVGPGSICTTRVVAGVGAPQITAILEAVAACGPAGVPVIADGGLQYSGDIAKALAAGASTAMLGSLLAGTAEAPGELIFVNGKQFKSYRGMGSLGAMAGRGSGGQAAKSYSKDRYFADDALSEDKLVPEGIEGRVPFRGPLSSVIHQLTGGLRAAMGYTGSPTIEALQQAQFVRITSAGLRESHPHDVAMTVEAPNYFAR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LZJL01000177
EMBL· GenBank· DDBJ
OBH22111.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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