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Protein

Imidazole glycerol phosphate synthase subunit HisH

Gene

hisH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR.

Catalytic activityi

5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide + L-glutamine = imidazole-glycerol phosphate + 5-aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H2O.1 Publication

Kineticsi

  1. KM=1.5 µM for glutamine1 Publication

    pH dependencei

    Optimum pH is 6-8.1 Publication

    Pathwayi: L-histidine biosynthesis

    This protein is involved in step 5 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
    Proteins known to be involved in the 9 steps of the subpathway in this organism are:
    1. ATP phosphoribosyltransferase (hisG)
    2. Histidine biosynthesis bifunctional protein HisIE (hisI)
    3. Histidine biosynthesis bifunctional protein HisIE (hisI)
    4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
    5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
    6. Histidine biosynthesis bifunctional protein HisB (hisB)
    7. Histidinol-phosphate aminotransferase (hisC)
    8. Histidine biosynthesis bifunctional protein HisB (hisB)
    9. Histidinol dehydrogenase (hisD)
    This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei77NucleophileBy similarity1
    Active sitei178By similarity1
    Active sitei180By similarity1

    GO - Molecular functioni

    • imidazoleglycerol-phosphate synthase activity Source: EcoCyc

    GO - Biological processi

    Keywordsi

    Molecular functionTransferase
    Biological processAmino-acid biosynthesis, Histidine biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:GLUTAMIDOTRANS-MONOMER
    MetaCyc:GLUTAMIDOTRANS-MONOMER
    BRENDAi4.3.1.B2 2026
    UniPathwayi
    UPA00031;UER00010

    Protein family/group databases

    MEROPSiC26.965

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Imidazole glycerol phosphate synthase subunit HisH (EC:2.4.2.-)
    Alternative name(s):
    IGP synthase glutamine amidotransferase subunit
    IGP synthase subunit HisH
    ImGP synthase subunit HisH
    Short name:
    IGPS subunit HisH
    Gene namesi
    Name:hisH
    Ordered Locus Names:b2023, JW2005
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10450 hisH

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001523731 – 196Imidazole glycerol phosphate synthase subunit HisHAdd BLAST196

    Proteomic databases

    EPDiP60595
    PaxDbiP60595
    PRIDEiP60595

    2D gel databases

    SWISS-2DPAGEiP60595

    Interactioni

    Subunit structurei

    Heterodimer of HisH and HisF.1 Publication

    Protein-protein interaction databases

    BioGridi4260419, 10 interactors
    IntActiP60595, 1 interactor
    STRINGi316385.ECDH10B_2171

    Structurei

    3D structure databases

    ProteinModelPortaliP60595
    SMRiP60595
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini2 – 196Glutamine amidotransferase type-1Add BLAST195

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4108UJE Bacteria
    COG0118 LUCA
    HOGENOMiHOG000025030
    InParanoidiP60595
    KOiK02501
    OMAiWVYFVHS
    PhylomeDBiP60595

    Family and domain databases

    CDDicd01748 GATase1_IGP_Synthase, 1 hit
    Gene3Di3.40.50.880, 1 hit
    HAMAPiMF_00278 HisH, 1 hit
    InterProiView protein in InterPro
    IPR029062 Class_I_gatase-like
    IPR017926 GATASE
    IPR010139 Imidazole-glycPsynth_HisH
    PANTHERiPTHR42701 PTHR42701, 1 hit
    PfamiView protein in Pfam
    PF00117 GATase, 1 hit
    PIRSFiPIRSF000495 Amidotransf_hisH, 1 hit
    SUPFAMiSSF52317 SSF52317, 1 hit
    TIGRFAMsiTIGR01855 IMP_synth_hisH, 1 hit
    PROSITEiView protein in PROSITE
    PS51273 GATASE_TYPE_1, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P60595-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNVVILDTGC ANLNSVKSAI ARHGYEPKVS RDPDVVLLAD KLFLPGVGTA
    60 70 80 90 100
    QAAMDQVRER ELFDLIKACT QPVLGICLGM QLLGRRSEES NGVDLLGIID
    110 120 130 140 150
    EDVPKMTDFG LPLPHMGWNR VYPQAGNRLF QGIEDGAYFY FVHSYAMPVN
    160 170 180 190
    PWTIAQCNYG EPFTAAVQKD NFYGVQFHPE RSGAAGAKLL KNFLEM
    Length:196
    Mass (Da):21,653
    Last modified:March 15, 2004 - v1
    Checksum:iB75A500ECD50DDD0
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X13462 Genomic DNA Translation: CAA31815.1
    U00096 Genomic DNA Translation: AAC75084.1
    AP009048 Genomic DNA Translation: BAA15854.1
    PIRiJS0132 XQECHH
    RefSeqiNP_416527.1, NC_000913.3
    WP_001103560.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC75084; AAC75084; b2023
    BAA15854; BAA15854; BAA15854
    GeneIDi946544
    KEGGiecj:JW2005
    eco:b2023
    PATRICifig|1411691.4.peg.229

    Similar proteinsi

    Entry informationi

    Entry nameiHIS5_ECOLI
    AccessioniPrimary (citable) accession number: P60595
    Secondary accession number(s): P10375
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: March 15, 2004
    Last modified: March 28, 2018
    This is version 117 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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