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Q9X0C6

- HIS6_THEMA

UniProt

Q9X0C6 - HIS6_THEMA

Protein

Imidazole glycerol phosphate synthase subunit HisF

Gene

hisF

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei11 – 111Sequence Analysis
    Active sitei130 – 1301Sequence Analysis

    GO - Molecular functioni

    1. imidazoleglycerol-phosphate synthase activity Source: UniProtKB-HAMAP
    2. lyase activity Source: UniProtKB-KW

    GO - Biological processi

    1. histidine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-467.
    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: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 – 139
    Beta strandi16 – 238
    Helixi32 – 4110
    Beta strandi46 – 538
    Beta strandi55 – 573
    Helixi58 – 7013
    Beta strandi77 – 826
    Helixi86 – 949
    Beta strandi98 – 1036
    Helixi104 – 1085
    Helixi111 – 12010
    Helixi122 – 1243
    Beta strandi125 – 13410
    Beta strandi137 – 1426
    Turni143 – 1464
    Beta strandi147 – 1526
    Helixi153 – 16210
    Beta strandi166 – 1727
    Turni173 – 1775
    Helixi184 – 1907
    Helixi191 – 1933
    Beta strandi198 – 2025
    Helixi207 – 2159
    Beta strandi219 – 2246
    Helixi225 – 2284
    Beta strandi229 – 2324
    Helixi234 – 24310
    Beta strandi250 – 2534

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK02500.
    OMAiDSYKVKQ.
    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

    MLAKRIIACL DVKDGRVVKG TNFENLRDSG DPVELGKFYS EIGIDELVFL    50
    DITASVEKRK TMLELVEKVA EQIDIPFTVG GGIHDFETAS ELILRGADKV 100
    SINTAAVENP SLITQIAQTF GSQAVVVAID AKRVDGEFMV FTYSGKKNTG 150
    ILLRDWVVEV EKRGAGEILL TSIDRDGTKS GYDTEMIRFV RPLTTLPIIA 200
    SGGAGKMEHF LEAFLAGADA ALAASVFHFR EIDVRELKEY LKKHGVNVRL 250
    EGL 253
    Length:253
    Mass (Da):27,719
    Last modified:November 1, 1999 - v1
    Checksum:iFE0F97F0C57E9025
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36113.1.
    PIRiC72304.
    RefSeqiNP_228842.1. NC_000853.1.
    YP_007977389.1. NC_021214.1.
    YP_008991868.1. NC_023151.1.

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36113.1 .
    PIRi C72304.
    RefSeqi NP_228842.1. NC_000853.1.
    YP_007977389.1. NC_021214.1.
    YP_008991868.1. NC_023151.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GPW X-ray 2.40 A/C/E 1-253 [» ]
    1THF X-ray 1.45 D 1-253 [» ]
    1VH7 X-ray 1.90 A 2-253 [» ]
    2A0N X-ray 1.64 A 1-253 [» ]
    2LLE NMR - A 103-247 [» ]
    2W6R X-ray 2.10 A 123-253 [» ]
    2WJZ X-ray 2.60 A/C/E 1-253 [» ]
    3CWO X-ray 3.10 X 103-253 [» ]
    3OG3 X-ray 2.08 A 43-221 [» ]
    3ZR4 X-ray 2.41 A/C/E 1-253 [» ]
    4EWN X-ray 1.90 D 1-253 [» ]
    4FX7 X-ray 2.08 A/B/C/D 99-219 [» ]
    4J9J X-ray 2.30 A 91-220 [» ]
    ProteinModelPortali Q9X0C6.
    SMRi Q9X0C6. Positions 1-251.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59020N.
    STRINGi 243274.TM1036.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD36113 ; AAD36113 ; TM_1036 .
    GeneIDi 897046.
    KEGGi tma:TM1036.
    tmi:THEMA_09180.
    tmm:Tmari_1040.
    PATRICi 23937001. VBITheMar51294_1049.

    Phylogenomic databases

    eggNOGi COG0107.
    KOi K02500.
    OMAi DSYKVKQ.
    OrthoDBi EOG6H1Q3W.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00010 .
    BioCyci MetaCyc:MONOMER-467.

    Miscellaneous databases

    EvolutionaryTracei Q9X0C6.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01013. HisF.
    InterProi IPR013785. Aldolase_TIM.
    IPR006062. His_biosynth.
    IPR004651. HisF.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    Pfami PF00977. His_biosynth. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 1 hit.
    TIGRFAMsi TIGR00735. hisF. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 107 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