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Protein

Imidazole glycerol phosphate synthase subunit HisH

Gene

hisH

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 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.

Enzyme regulationi

Activated by the binding of either IGP or PRFAR to the active site of HisF.

Kineticsi

  1. KM=0.32 mM for glutamine1 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), 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 (Tmari_1041), 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), 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), Histidinol-phosphate aminotransferase (Tmari_1044)
    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 sitei84 – 841Nucleophile
    Active sitei178 – 1781
    Active sitei180 – 1801

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-468.
    BRENDAi4.3.1.B2. 6331.
    UniPathwayiUPA00031; 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
    TmHisH
    Gene namesi
    Name:hisH
    Ordered Locus Names:TM_1038
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    Proteomesi
    • UP000008183 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201Imidazole glycerol phosphate synthase subunit HisHPRO_0000152437Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of HisH and HisF.

    Protein-protein interaction databases

    DIPiDIP-59019N.
    STRINGi243274.TM1038.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Beta strandi9 – 113Combined sources
    Helixi14 – 2310Combined sources
    Turni24 – 263Combined sources
    Beta strandi27 – 293Combined sources
    Beta strandi31 – 355Combined sources
    Beta strandi44 – 485Combined sources
    Helixi55 – 639Combined sources
    Helixi67 – 759Combined sources
    Beta strandi79 – 835Combined sources
    Helixi85 – 884Combined sources
    Beta strandi91 – 944Combined sources
    Beta strandi97 – 1015Combined sources
    Beta strandi105 – 1128Combined sources
    Beta strandi119 – 13214Combined sources
    Beta strandi135 – 14713Combined sources
    Helixi149 – 1513Combined sources
    Beta strandi152 – 1587Combined sources
    Beta strandi161 – 1699Combined sources
    Beta strandi172 – 1776Combined sources
    Helixi179 – 1813Combined sources
    Helixi183 – 19614Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GPWX-ray2.40B/D/F1-201[»]
    1K9VX-ray2.40F1-201[»]
    1KXJX-ray2.80A/B1-201[»]
    2WJZX-ray2.60B/D/F1-201[»]
    3ZR4X-ray2.41B/D/F1-201[»]
    ProteinModelPortaliQ9X0C8.
    SMRiQ9X0C8. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X0C8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 201200Glutamine amidotransferase type-1Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4108UJE. Bacteria.
    COG0118. LUCA.
    InParanoidiQ9X0C8.
    KOiK02501.
    OMAiSTIAQCH.
    OrthoDBiEOG69KV05.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    HAMAPiMF_00278. HisH.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR010139. Imidazole-glycPsynth_HisH.
    [Graphical view]
    PfamiPF00117. GATase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000495. Amidotransf_hisH. 1 hit.
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR01855. IMP_synth_hisH. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9X0C8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRIGIISVGP GNIMNLYRGV KRASENFEDV SIELVESPRN DLYDLLFIPG
    60 70 80 90 100
    VGHFGEGMRR LRENDLIDFV RKHVEDERYV VGVCLGMQLL FEESEEAPGV
    110 120 130 140 150
    KGLSLIEGNV VKLRSRRLPH MGWNEVIFKD TFPNGYYYFV HTYRAVCEEE
    160 170 180 190 200
    HVLGTTEYDG EIFPSAVRKG RILGFQFHPE KSSKIGRKLL EKVIECSLSR

    R
    Length:201
    Mass (Da):23,097
    Last modified:November 1, 1999 - v1
    Checksum:i10957D075094F778
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36115.1.
    PIRiE72304.
    RefSeqiNP_228844.1. NC_000853.1.
    WP_004080484.1. NZ_CP011107.1.

    Genome annotation databases

    EnsemblBacteriaiAAD36115; AAD36115; TM_1038.
    GeneIDi897045.
    KEGGitma:TM1038.
    PATRICi23937005. VBITheMar51294_1051.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD36115.1.
    PIRiE72304.
    RefSeqiNP_228844.1. NC_000853.1.
    WP_004080484.1. NZ_CP011107.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GPWX-ray2.40B/D/F1-201[»]
    1K9VX-ray2.40F1-201[»]
    1KXJX-ray2.80A/B1-201[»]
    2WJZX-ray2.60B/D/F1-201[»]
    3ZR4X-ray2.41B/D/F1-201[»]
    ProteinModelPortaliQ9X0C8.
    SMRiQ9X0C8. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-59019N.
    STRINGi243274.TM1038.

    Protein family/group databases

    MEROPSiC26.965.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD36115; AAD36115; TM_1038.
    GeneIDi897045.
    KEGGitma:TM1038.
    PATRICi23937005. VBITheMar51294_1051.

    Phylogenomic databases

    eggNOGiENOG4108UJE. Bacteria.
    COG0118. LUCA.
    InParanoidiQ9X0C8.
    KOiK02501.
    OMAiSTIAQCH.
    OrthoDBiEOG69KV05.

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00010.
    BioCyciMetaCyc:MONOMER-468.
    BRENDAi4.3.1.B2. 6331.

    Miscellaneous databases

    EvolutionaryTraceiQ9X0C8.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    HAMAPiMF_00278. HisH.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR010139. Imidazole-glycPsynth_HisH.
    [Graphical view]
    PfamiPF00117. GATase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000495. Amidotransf_hisH. 1 hit.
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR01855. IMP_synth_hisH. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]
    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, BIOPHYSICOCHEMICAL PROPERTIES.
    3. "Crystal structure of glutamine amidotransferase from Thermotoga maritima."
      Korolev S., Skarina T., Evdokimova E., Beasley S., Edwards A., Joachimiak A., Savchenko A.
      Proteins 49:420-422(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 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 nameiHIS5_THEMA
    AccessioniPrimary (citable) accession number: Q9X0C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: November 1, 1999
    Last modified: April 13, 2016
    This is version 126 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

    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.