A0A3S4HSG8 · A0A3S4HSG8_AVIVO

Function

function

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.

Catalytic activity

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site78Nucleophile
Active site178
Active site180

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglutaminase activity
Molecular Functionimidazoleglycerol-phosphate synthase activity
Molecular Functionlyase activity
Biological Processglutamine metabolic process
Biological ProcessL-histidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Imidazole glycerol phosphate synthase subunit HisH
  • EC number
  • Alternative names
    • IGP synthase glutaminase subunit
      (EC:3.5.1.2
      ) . EC:3.5.1.2 (UniProtKB | ENZYME | Rhea)
    • IGP synthase subunit HisH
    • ImGP synthase subunit HisH
      (IGPS subunit HisH
      )

Gene names

    • Name
      hisH
    • ORF names
      NCTC3438_00680

Organism names

Accessions

  • Primary accession
    A0A3S4HSG8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Heterodimer of HisH and HisF.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-195Glutamine amidotransferase

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    197
  • Mass (Da)
    22,013
  • Last updated
    2019-04-10 v1
  • Checksum
    F609626F67E699D6
MNNITIINTGCANLSSVKFAFERLGYQAEITDDLAKIQSAEKLILPGVGTASAAMQSMQSRQLIETIQQLTQPVLGICLGMQLMTDFSAEGEIETLRLINGNTQRLPNKGLPLPHMGWNKVHYQDNHPLFIDIPQDSYFYFVHSYAVLPNENTIATCDYGVPFSAAIARNNFYGVQFHPERSGKVGEQLLRNFMENL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR134167
EMBL· GenBank· DDBJ
VEB22847.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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