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Protein

Imidazole glycerol phosphate synthase subunit HisF

Gene

hisF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.

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=240 µM for PRFAR1 Publication
  2. KM=23 µM for NH4Cl1 Publication

    pH dependencei

    Optimum pH is 8-9.1 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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei11 – 111Sequence analysis
    Active sitei130 – 1301Sequence analysis

    GO - Molecular functioni

    • imidazoleglycerol-phosphate synthase activity Source: EcoCyc
    • lyase activity Source: UniProtKB-KW

    GO - Biological processi

    • histidine biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:CYCLASE-MONOMER.
    ECOL316407:JW2007-MONOMER.
    MetaCyc:CYCLASE-MONOMER.
    BRENDAi4.3.1.B2. 2026.
    UniPathwayiUPA00031; UER00010.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Imidazole glycerol phosphate synthase subunit HisF (EC:4.1.3.-)
    Alternative name(s):
    IGP synthase cyclase subunit
    IGP synthase subunit HisF
    ImGP synthase subunit HisF
    Short name:
    IGPS subunit HisF
    Gene namesi
    Name:hisF
    Ordered Locus Names:b2025, JW2007
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10448. hisF.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    • imidazoleglycerol-phosphate synthase complex Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 51R → A: Loss of activity. 1 Publication
    Mutagenesisi5 – 51R → H: Loss of IGP synthase activity. Weak IGP synthase activity and reduced HisH activity in vitro. 1 Publication
    Mutagenesisi46 – 461E → A: Loss of activity. 1 Publication
    Mutagenesisi46 – 461E → G: Loss of IGP synthase activity. Weak IGP synthase and HisH activities in vitro. 1 Publication
    Mutagenesisi123 – 1231Q → A: Decrease in activity. 1 Publication
    Mutagenesisi123 – 1231Q → R: Loss of IGP synthase activity. Weak HisH activity in vitro. 1 Publication
    Mutagenesisi124 – 1241C → A: No change in activity. 1 Publication
    Mutagenesisi124 – 1241C → R: Loss of IGP synthase activity. Weak HisH activity in vitro. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 258258Imidazole glycerol phosphate synthase subunit HisFPRO_0000142156Add
    BLAST

    Proteomic databases

    EPDiP60664.
    PaxDbiP60664.
    PRIDEiP60664.

    Interactioni

    Subunit structurei

    Heterodimer of HisH and HisF.1 Publication

    Protein-protein interaction databases

    BioGridi4259164. 5 interactions.
    IntActiP60664. 4 interactions.
    STRINGi511145.b2025.

    Structurei

    3D structure databases

    ProteinModelPortaliP60664.
    SMRiP60664. Positions 2-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HisA/HisF family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C0S. Bacteria.
    COG0107. LUCA.
    HOGENOMiHOG000224612.
    InParanoidiP60664.
    KOiK02500.
    OMAiKGTNFVN.
    PhylomeDBiP60664.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01013. HisF. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR006062. His_biosynth.
    IPR004651. HisF.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00977. His_biosynth. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.
    TIGRFAMsiTIGR00735. hisF. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P60664-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLAKRIIPCL DVRDGQVVKG VQFRNHEIIG DIVPLAKRYA EEGADELVFY
    60 70 80 90 100
    DITASSDGRV VDKSWVSRVA EVIDIPFCVA GGIKSLEDAA KILSFGADKI
    110 120 130 140 150
    SINSPALADP TLITRLADRF GVQCIVVGID TWYDAETGKY HVNQYTGDES
    160 170 180 190 200
    RTRVTQWETL DWVQEVQKRG AGEIVLNMMN QDGVRNGYDL EQLKKVREVC
    210 220 230 240 250
    HVPLIASGGA GTMEHFLEAF RDADVDGALA ASVFHKQIIN IGELKAYLAT

    QGVEIRIC
    Length:258
    Mass (Da):28,454
    Last modified:March 29, 2004 - v1
    Checksum:iFCE14A345521BEA1
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X13462 Genomic DNA. Translation: CAA31817.1.
    U00096 Genomic DNA. Translation: AAC75086.1.
    AP009048 Genomic DNA. Translation: BAA15857.1.
    D43637 Genomic DNA. Translation: BAA07754.1.
    PIRiJS0134. OYECHF.
    RefSeqiNP_416529.1. NC_000913.3.
    WP_000880182.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75086; AAC75086; b2025.
    BAA15857; BAA15857; BAA15857.
    GeneIDi946516.
    KEGGiecj:JW2007.
    eco:b2025.
    PATRICi32119385. VBIEscCol129921_2102.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X13462 Genomic DNA. Translation: CAA31817.1.
    U00096 Genomic DNA. Translation: AAC75086.1.
    AP009048 Genomic DNA. Translation: BAA15857.1.
    D43637 Genomic DNA. Translation: BAA07754.1.
    PIRiJS0134. OYECHF.
    RefSeqiNP_416529.1. NC_000913.3.
    WP_000880182.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP60664.
    SMRiP60664. Positions 2-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259164. 5 interactions.
    IntActiP60664. 4 interactions.
    STRINGi511145.b2025.

    Proteomic databases

    EPDiP60664.
    PaxDbiP60664.
    PRIDEiP60664.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75086; AAC75086; b2025.
    BAA15857; BAA15857; BAA15857.
    GeneIDi946516.
    KEGGiecj:JW2007.
    eco:b2025.
    PATRICi32119385. VBIEscCol129921_2102.

    Organism-specific databases

    EchoBASEiEB0443.
    EcoGeneiEG10448. hisF.

    Phylogenomic databases

    eggNOGiENOG4105C0S. Bacteria.
    COG0107. LUCA.
    HOGENOMiHOG000224612.
    InParanoidiP60664.
    KOiK02500.
    OMAiKGTNFVN.
    PhylomeDBiP60664.

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00010.
    BioCyciEcoCyc:CYCLASE-MONOMER.
    ECOL316407:JW2007-MONOMER.
    MetaCyc:CYCLASE-MONOMER.
    BRENDAi4.3.1.B2. 2026.

    Miscellaneous databases

    PROiP60664.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01013. HisF. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR006062. His_biosynth.
    IPR004651. HisF.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00977. His_biosynth. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.
    TIGRFAMsiTIGR00735. hisF. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHIS6_ECOLI
    AccessioniPrimary (citable) accession number: P60664
    Secondary accession number(s): P10373
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: March 29, 2004
    Last modified: September 7, 2016
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.