Q31E66 · HIS5_HYDCU

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 site86Nucleophile
Active site192
Active site194

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
    • Ordered locus names
      Tcr_1967

Organism names

Accessions

  • Primary accession
    Q31E66

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002317671-213Imidazole glycerol phosphate synthase subunit HisH

Interaction

Subunit

Heterodimer of HisH and HisF.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-213Glutamine amidotransferase type-1

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    213
  • Mass (Da)
    23,666
  • Last updated
    2005-12-06 v1
  • Checksum
    B106D7F4F9E03E71
MTDQKLVTVIDYGMGNLRSVAKAAEHAADSNTRICISDKAEDIRSADAIIFPGQGAAKACMKALNETNITHALIQAATEKPFLGICMGLQVLMTHSQENEGVDCLDILKGDVQKFDLSGHPELKMPHMGWNQIHQTIDHPLWHNIEQNSRFYFVHSYFVSPHDKQIIAGETTHGKRFTSAIAQNNLFAIQAHPEKSADAGLQLFKNFLNWNGQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000109
EMBL· GenBank· DDBJ
ABB42557.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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