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Protein

Histidine biosynthesis bifunctional protein HisB

Gene

hisB

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
    Active sitei9NucleophileUniRule annotation1 Publication1
    Metal bindingi9MagnesiumUniRule annotation1 Publication1
    Active sitei11Proton donorUniRule annotation1 Publication1
    Metal bindingi11Magnesium; via carbonyl oxygenUniRule annotation1 Publication1
    Metal bindingi93ZincUniRule annotation1 Publication1
    Metal bindingi95Zinc; via pros nitrogenUniRule annotation1 Publication1
    Metal bindingi101ZincUniRule annotation1 Publication1
    Metal bindingi103ZincUniRule annotation1 Publication1
    Metal bindingi130MagnesiumUniRule annotation1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase, Lyase, Multifunctional enzyme
    Biological processAmino-acid biosynthesis, Histidine biosynthesis
    LigandMagnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi17E → A: Severe decrease in histidinol-phosphate phosphatase activity in presence of low magnesium concentration. At higher magnesium concentration (5mM), no effect on activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001582081 – 355Histidine biosynthesis bifunctional protein HisBAdd BLAST355

    Interactioni

    Protein-protein interaction databases

    STRINGi155864.Z3184

    Structurei

    Secondary structure

    1355
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 8Combined sources5
    Turni12 – 14Combined sources3
    Turni19 – 21Combined sources3
    Helixi27 – 29Combined sources3
    Helixi36 – 45Combined sources10
    Beta strandi48 – 55Combined sources8
    Turni57 – 60Combined sources4
    Helixi66 – 82Combined sources17
    Beta strandi87 – 93Combined sources7
    Helixi97 – 99Combined sources3
    Beta strandi102 – 104Combined sources3
    Helixi109 – 114Combined sources6
    Helixi122 – 124Combined sources3
    Beta strandi126 – 131Combined sources6
    Helixi132 – 141Combined sources10
    Beta strandi143 – 147Combined sources5
    Turni150 – 152Combined sources3
    Helixi155 – 161Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9S5G5

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 166Histidinol-phosphataseUniRule annotation1 PublicationAdd BLAST166
    Regioni167 – 355Imidazoleglycerol-phosphate dehydrataseUniRule annotationBy similarityAdd BLAST189

    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

    Family and domain databases

    CDDicd07914 IGPD, 1 hit
    Gene3Di3.30.230.40, 2 hits
    3.40.50.1000, 1 hit
    HAMAPiMF_01022 Bifunc_HisB, 1 hit
    MF_00076 HisB, 1 hit
    InterProiView protein in InterPro
    IPR036412 HAD-like_sf
    IPR006549 HAD-SF_hydro_IIIA
    IPR023214 HAD_sf
    IPR020566 His_synth_bifunc_HisB
    IPR005954 HisB_N
    IPR006543 Histidinol-phos
    IPR038494 IGPD_sf
    IPR000807 ImidazoleglycerolP_deHydtase
    IPR020565 ImidazoleglycerP_deHydtase_CS
    IPR013954 PNK3P
    IPR020568 Ribosomal_S5_D2-typ_fold
    PANTHERiPTHR23133 PTHR23133, 1 hit
    PfamiView protein in Pfam
    PF00475 IGPD, 1 hit
    PF08645 PNK3P, 1 hit
    SUPFAMiSSF54211 SSF54211, 2 hits
    SSF56784 SSF56784, 1 hit
    TIGRFAMsiTIGR01662 HAD-SF-IIIA, 1 hit
    TIGR01261 hisB_Nterm, 1 hit
    TIGR01656 Histidinol-ppas, 1 hit
    PROSITEiView protein in PROSITE
    PS00954 IGP_DEHYDRATASE_1, 1 hit
    PS00955 IGP_DEHYDRATASE_2, 1 hit

    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 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence BAB36246 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_NOKN01000002.1

    Genome annotation databases

    EnsemblBacteriaiAAG57081; AAG57081; Z3184
    BAB36246; BAB36246; BAB36246
    GeneIDi914091
    KEGGiece:Z3184
    ecs:ECs2823
    PATRICifig|386585.9.peg.2958

    Similar proteinsi

    Entry informationi

    Entry nameiHIS7_ECO57
    AccessioniPrimary (citable) accession number: Q9S5G5
    Secondary accession number(s): Q8X8T1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 24, 2002
    Last sequence update: May 1, 2000
    Last modified: April 25, 2018
    This is version 120 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

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