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Protein

Histidine biosynthesis bifunctional protein HisB

Gene

hisB

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O.UniRule annotation
L-histidinol phosphate + H2O = L-histidinol + phosphate.UniRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation1 PublicationNote: Binds 2 Mg2+ ions. Also can use Co2+ and Mn2+ions.1 Publication
  • Zn2+UniRule annotation1 Publication

Enzyme regulationi

Inhibited by Ca2+.1 Publication

Kineticsi

  1. KM=54 µM for histidinol phosphate (in the presence of Mg2+)1 Publication
  2. KM=54 µM for histidinol phosphate (in the presence of Co2+)1 Publication
  3. KM=41 µM for histidinol phosphate (in the presence of Zn2+)1 Publication
  4. KM=52 µM for histidinol phosphate (in the presence of Mn2+)1 Publication

    Pathwayi: L-histidine biosynthesis

    This protein is involved in step 6 and 8 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
    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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
    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 sitei9 – 91NucleophileUniRule annotation1 Publication
    Metal bindingi9 – 91MagnesiumUniRule annotation1 Publication
    Active sitei11 – 111Proton donorUniRule annotation1 Publication
    Metal bindingi11 – 111Magnesium; via carbonyl oxygenUniRule annotation1 Publication
    Metal bindingi93 – 931ZincUniRule annotation1 Publication
    Metal bindingi95 – 951Zinc; via pros nitrogenUniRule annotation1 Publication
    Metal bindingi101 – 1011ZincUniRule annotation1 Publication
    Metal bindingi103 – 1031ZincUniRule annotation1 Publication
    Metal bindingi130 – 1301MagnesiumUniRule annotation1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Keywords - Molecular functioni

    Hydrolase, Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-2787-MONOMER.
    UniPathwayiUPA00031; UER00011.
    UPA00031; UER00013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histidine biosynthesis bifunctional protein HisBUniRule annotation
    Including the following 2 domains:
    Histidinol-phosphataseUniRule annotation (EC:3.1.3.15UniRule annotation1 Publication)
    Alternative name(s):
    Histidinol-phosphate phosphatase1 Publication
    Imidazoleglycerol-phosphate dehydrataseUniRule annotation (EC:4.2.1.19UniRule annotation)
    Short name:
    IGPDUniRule annotation
    Gene namesi
    Name:hisBUniRule annotation
    Ordered Locus Names:Z3184, ECs2823
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000558 Componenti: Chromosome
    • UP000002519 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171E → A: Severe decrease in histidinol-phosphate phosphatase activity in presence of low magnesium concentration. At higher magnesium concentration (5mM), no effect on activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 355355Histidine biosynthesis bifunctional protein HisBPRO_0000158208Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi155864.Z3184.

    Structurei

    Secondary structure

    1
    355
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85Combined sources
    Turni12 – 143Combined sources
    Turni19 – 213Combined sources
    Helixi27 – 293Combined sources
    Helixi36 – 4510Combined sources
    Beta strandi48 – 558Combined sources
    Turni57 – 604Combined sources
    Helixi66 – 8217Combined sources
    Beta strandi87 – 937Combined sources
    Helixi97 – 993Combined sources
    Beta strandi102 – 1043Combined sources
    Helixi109 – 1146Combined sources
    Helixi122 – 1243Combined sources
    Beta strandi126 – 1316Combined sources
    Helixi132 – 14110Combined sources
    Beta strandi143 – 1475Combined sources
    Turni150 – 1523Combined sources
    Helixi155 – 1617Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FPRX-ray1.70A/B2-165[»]
    2FPSX-ray2.20A/B2-165[»]
    2FPUX-ray1.80A/B2-165[»]
    2FPWX-ray1.75A/B2-165[»]
    2FPXX-ray1.80A/B2-165[»]
    ProteinModelPortaliQ9S5G5.
    SMRiQ9S5G5. Positions 3-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9S5G5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 166166Histidinol-phosphataseUniRule annotation1 PublicationAdd
    BLAST
    Regioni167 – 355189Imidazoleglycerol-phosphate dehydrataseUniRule annotationBy similarityAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the histidinol-phosphatase family.UniRule annotation
    In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105ECC. Bacteria.
    COG0131. LUCA.
    COG0241. LUCA.
    HOGENOMiHOG000228065.
    KOiK01089.
    OMAiPEDTFWP.
    OrthoDBiEOG60PHGP.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    HAMAPiMF_00076. HisB.
    MF_01022. Bifunc_HisB.
    InterProiIPR023214. HAD-like_dom.
    IPR006549. HAD-SF_hydro_IIIA.
    IPR020566. His_synth_bifunc_HisB.
    IPR005954. HisB_N.
    IPR006543. Histidinol-phos.
    IPR000807. ImidazoleglycerolP_deHydtase.
    IPR020565. ImidazoleglycerP_deHydtase_CS.
    IPR013954. PNK3P.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PANTHERiPTHR23133:SF2. PTHR23133:SF2. 2 hits.
    PfamiPF00475. IGPD. 1 hit.
    PF08645. PNK3P. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 2 hits.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
    TIGR01261. hisB_Nterm. 1 hit.
    TIGR01656. Histidinol-ppas. 1 hit.
    PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
    PS00955. IGP_DEHYDRATASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9S5G5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSQKYLFIDR DGTLISEPPS DFQVDRFDKL AFEPGVIPQL LKLQKAGYKL
    60 70 80 90 100
    VMITNQDGLG TQSFPQADFD GPHNLMMQIF TSQGVQFDEV LICPHLPADE
    110 120 130 140 150
    CDCRKPKVKL VERYLAEQAM DRANSYVIGD RATDIQLAEN MGINGLRYDR
    160 170 180 190 200
    ETLNWPMIGE QLTRRDRYAH VVRNTKETQI DVQVWLDREG GSKINTGVGF
    210 220 230 240 250
    FDHMLDQIAT HGGFRMEINV KGDLYIDDHH TVEDTGLALG EALKIALGDK
    260 270 280 290 300
    RGICRFGFVL PMDECLARCA LDISGRPHLE YKAEFTYQRV GDLSTEMIEH
    310 320 330 340 350
    FFRSLSYTMG VTLHLKTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS

    SKGVL
    Length:355
    Mass (Da):40,290
    Last modified:May 1, 2000 - v1
    Checksum:i91229A10D62A4EE8
    GO

    Sequence cautioni

    The sequence AAG57081.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAB36246.1 differs from that shown. Reason: Erroneous initiation. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB008676 Genomic DNA. Translation: BAA77743.1.
    AE005174 Genomic DNA. Translation: AAG57081.1. Different initiation.
    BA000007 Genomic DNA. Translation: BAB36246.1. Different initiation.
    PIRiE85827.
    G90981.
    RefSeqiNP_310850.2. NC_002695.1.
    WP_000080139.1. NZ_LPWC01000508.1.

    Genome annotation databases

    EnsemblBacteriaiAAG57081; AAG57081; Z3184.
    BAB36246; BAB36246; BAB36246.
    GeneIDi914091.
    KEGGiece:Z3184.
    ecs:ECs2823.
    PATRICi18355034. VBIEscCol44059_2718.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB008676 Genomic DNA. Translation: BAA77743.1.
    AE005174 Genomic DNA. Translation: AAG57081.1. Different initiation.
    BA000007 Genomic DNA. Translation: BAB36246.1. Different initiation.
    PIRiE85827.
    G90981.
    RefSeqiNP_310850.2. NC_002695.1.
    WP_000080139.1. NZ_LPWC01000508.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FPRX-ray1.70A/B2-165[»]
    2FPSX-ray2.20A/B2-165[»]
    2FPUX-ray1.80A/B2-165[»]
    2FPWX-ray1.75A/B2-165[»]
    2FPXX-ray1.80A/B2-165[»]
    ProteinModelPortaliQ9S5G5.
    SMRiQ9S5G5. Positions 3-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi155864.Z3184.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG57081; AAG57081; Z3184.
    BAB36246; BAB36246; BAB36246.
    GeneIDi914091.
    KEGGiece:Z3184.
    ecs:ECs2823.
    PATRICi18355034. VBIEscCol44059_2718.

    Phylogenomic databases

    eggNOGiENOG4105ECC. Bacteria.
    COG0131. LUCA.
    COG0241. LUCA.
    HOGENOMiHOG000228065.
    KOiK01089.
    OMAiPEDTFWP.
    OrthoDBiEOG60PHGP.

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00011.
    UPA00031; UER00013.
    BioCyciECOL386585:GJFA-2787-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ9S5G5.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    HAMAPiMF_00076. HisB.
    MF_01022. Bifunc_HisB.
    InterProiIPR023214. HAD-like_dom.
    IPR006549. HAD-SF_hydro_IIIA.
    IPR020566. His_synth_bifunc_HisB.
    IPR005954. HisB_N.
    IPR006543. Histidinol-phos.
    IPR000807. ImidazoleglycerolP_deHydtase.
    IPR020565. ImidazoleglycerP_deHydtase_CS.
    IPR013954. PNK3P.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    [Graphical view]
    PANTHERiPTHR23133:SF2. PTHR23133:SF2. 2 hits.
    PfamiPF00475. IGPD. 1 hit.
    PF08645. PNK3P. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 2 hits.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
    TIGR01261. hisB_Nterm. 1 hit.
    TIGR01656. Histidinol-ppas. 1 hit.
    PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
    PS00955. IGP_DEHYDRATASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157."
      Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.
      Microb. Pathog. 26:235-247(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: O157:H- / 184 / EHEC.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    3. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
    4. "Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway."
      Rangarajan E.S., Proteau A., Wagner J., Hung M.N., Matte A., Cygler M.
      J. Biol. Chem. 281:37930-37941(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-165 IN COMPLEX WITH CALCIUM; MAGNESIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, REGION, MUTAGENESIS OF GLU-17.

    Entry informationi

    Entry nameiHIS7_ECO57
    AccessioniPrimary (citable) accession number: Q9S5G5
    Secondary accession number(s): Q8X8T1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 24, 2002
    Last sequence update: May 1, 2000
    Last modified: May 11, 2016
    This is version 108 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, Multifunctional enzyme

    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.