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Protein

Imidazole glycerol phosphate synthase subunit HisF

Gene

hisF

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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.

Kineticsi

  1. KM=1.5 µM for PRFAR1 Publication
  2. KM=2.2 mM for NH31 Publication

    Pathway:iL-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 (Tmari_1046), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
    2. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
    3. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
    4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
    5. Imidazole glycerol phosphate synthase amidotransferase subunit (Tmari_1042), Imidazole glycerol phosphate synthase cyclase subunit (Tmari_1040), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
    6. Imidazoleglycerol-phosphate dehydratase (Tmari_1043), Imidazoleglycerol-phosphate dehydratase (hisB)
    7. Histidinol-phosphate aminotransferase (hisC)
    8. Probable histidinol-phosphatase (hisK)
    9. Histidinol dehydrogenase (Tmari_1045), 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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-467.
    BRENDAi4.3.1.B2. 6331.
    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:TM_1036
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91C → A: No change in activity. 1 Publication
    Mutagenesisi11 – 111D → X: Loss of activity. 1 Publication
    Mutagenesisi19 – 191K → S: Decrease in activity. 1 Publication
    Mutagenesisi51 – 511D → N: No change in activity. 1 Publication
    Mutagenesisi103 – 1031N → A: No change in activity. 1 Publication
    Mutagenesisi130 – 1301D → A, C, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W or Y: Complete loss of activity. 1 Publication
    Mutagenesisi130 – 1301D → E: Weak activity. 1 Publication
    Mutagenesisi176 – 1761D → N: Decrease in activity. 1 Publication
    Mutagenesisi183 – 1831D → N: No change in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 253253Imidazole glycerol phosphate synthase subunit HisFPRO_0000142253Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of HisH and HisF.

    Protein-protein interaction databases

    DIPiDIP-59020N.
    STRINGi243274.TM1036.

    Structurei

    Secondary structure

    1
    253
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139Combined sources
    Beta strandi16 – 238Combined sources
    Helixi32 – 4110Combined sources
    Beta strandi46 – 538Combined sources
    Beta strandi55 – 573Combined sources
    Helixi58 – 7013Combined sources
    Beta strandi77 – 826Combined sources
    Helixi86 – 949Combined sources
    Beta strandi98 – 1036Combined sources
    Helixi104 – 1085Combined sources
    Helixi111 – 12010Combined sources
    Helixi122 – 1243Combined sources
    Beta strandi125 – 13410Combined sources
    Beta strandi137 – 1426Combined sources
    Turni143 – 1464Combined sources
    Beta strandi147 – 1526Combined sources
    Helixi153 – 16210Combined sources
    Beta strandi166 – 1727Combined sources
    Turni173 – 1775Combined sources
    Helixi184 – 1907Combined sources
    Helixi191 – 1933Combined sources
    Beta strandi198 – 2025Combined sources
    Helixi207 – 2159Combined sources
    Beta strandi219 – 2246Combined sources
    Helixi225 – 2284Combined sources
    Beta strandi229 – 2324Combined sources
    Helixi234 – 24310Combined sources
    Beta strandi250 – 2534Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GPWX-ray2.40A/C/E1-253[»]
    1THFX-ray1.45D1-253[»]
    1VH7X-ray1.90A2-253[»]
    2A0NX-ray1.64A1-253[»]
    2LLENMR-A103-247[»]
    2W6RX-ray2.10A123-253[»]
    2WJZX-ray2.60A/C/E1-253[»]
    3CWOX-ray3.10X103-253[»]
    3OG3X-ray2.08A43-221[»]
    3ZR4X-ray2.41A/C/E1-253[»]
    4EWNX-ray1.90D1-253[»]
    4FX7X-ray2.08A/B/C/D99-219[»]
    4J9JX-ray2.30A91-220[»]
    ProteinModelPortaliQ9X0C6.
    SMRiQ9X0C6. Positions 1-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X0C6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HisA/HisF family.Curated

    Phylogenomic databases

    eggNOGiCOG0107.
    InParanoidiQ9X0C6.
    KOiK02500.
    OMAiVFHFGEI.
    OrthoDBiEOG6H1Q3W.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01013. HisF.
    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.

    Q9X0C6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLAKRIIACL DVKDGRVVKG TNFENLRDSG DPVELGKFYS EIGIDELVFL
    60 70 80 90 100
    DITASVEKRK TMLELVEKVA EQIDIPFTVG GGIHDFETAS ELILRGADKV
    110 120 130 140 150
    SINTAAVENP SLITQIAQTF GSQAVVVAID AKRVDGEFMV FTYSGKKNTG
    160 170 180 190 200
    ILLRDWVVEV EKRGAGEILL TSIDRDGTKS GYDTEMIRFV RPLTTLPIIA
    210 220 230 240 250
    SGGAGKMEHF LEAFLAGADA ALAASVFHFR EIDVRELKEY LKKHGVNVRL

    EGL
    Length:253
    Mass (Da):27,719
    Last modified:November 1, 1999 - v1
    Checksum:iFE0F97F0C57E9025
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36113.1.
    PIRiC72304.
    RefSeqiNP_228842.1. NC_000853.1.
    WP_004080486.1. NZ_CP011107.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36113; AAD36113; TM_1036.
    GeneIDi897046.
    KEGGitma:TM1036.
    tmi:THEMA_09180.
    tmm:Tmari_1040.
    PATRICi23937001. VBITheMar51294_1049.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36113.1.
    PIRiC72304.
    RefSeqiNP_228842.1. NC_000853.1.
    WP_004080486.1. NZ_CP011107.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GPWX-ray2.40A/C/E1-253[»]
    1THFX-ray1.45D1-253[»]
    1VH7X-ray1.90A2-253[»]
    2A0NX-ray1.64A1-253[»]
    2LLENMR-A103-247[»]
    2W6RX-ray2.10A123-253[»]
    2WJZX-ray2.60A/C/E1-253[»]
    3CWOX-ray3.10X103-253[»]
    3OG3X-ray2.08A43-221[»]
    3ZR4X-ray2.41A/C/E1-253[»]
    4EWNX-ray1.90D1-253[»]
    4FX7X-ray2.08A/B/C/D99-219[»]
    4J9JX-ray2.30A91-220[»]
    ProteinModelPortaliQ9X0C6.
    SMRiQ9X0C6. Positions 1-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-59020N.
    STRINGi243274.TM1036.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD36113; AAD36113; TM_1036.
    GeneIDi897046.
    KEGGitma:TM1036.
    tmi:THEMA_09180.
    tmm:Tmari_1040.
    PATRICi23937001. VBITheMar51294_1049.

    Phylogenomic databases

    eggNOGiCOG0107.
    InParanoidiQ9X0C6.
    KOiK02500.
    OMAiVFHFGEI.
    OrthoDBiEOG6H1Q3W.

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00010.
    BioCyciMetaCyc:MONOMER-467.
    BRENDAi4.3.1.B2. 6331.

    Miscellaneous databases

    EvolutionaryTraceiQ9X0C6.
    PROiQ9X0C6.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01013. HisF.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex."
      Beismann-Driemeyer S., Sterner R.
      J. Biol. Chem. 276:20387-20396(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF CYS-9; ASP-11; LYS-19; ASP-51; ASN-103; ASP-130; ASP-176 AND ASP-183, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
    3. "Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion."
      Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.
      Science 289:1546-1550(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
    4. "Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex."
      Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M.C., Sterner R., Wilmanns M.
      Structure 10:185-193(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiHIS6_THEMA
    AccessioniPrimary (citable) accession number: Q9X0C6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: November 1, 1999
    Last modified: July 22, 2015
    This is version 116 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.