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Protein

D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase

Gene

BB4091

Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.2 Publications

Catalytic activityi

D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate.1 Publication

Cofactori

Protein has several cofactor binding sites:

Kineticsi

kcat is 22 sec(-1) and 5.9 sec(-1) with beta-HBP and alpha-HBP as substrate, respectively. Thus, the enzyme displays 150-fold more efficiency towards the beta- than the alpha-anomer (PubMed:20050615).1 Publication

  1. KM=6.9 µM for beta-HBP (at pH 7.5 and 25 degrees Celsius)1 Publication
  2. KM=280 µM for alpha-HBP (at pH 7.5 and 25 degrees Celsius)1 Publication

    Pathwayi: ADP-L-glycero-beta-D-manno-heptose biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate.1 Publication
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. D-beta-D-heptose 7-phosphate kinase (rfaE)
    2. D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (BB4091)
    3. D-beta-D-heptose 1-phosphate adenylyltransferase (BB4463)
    4. ADP-L-glycero-D-manno-heptose-6-epimerase (hldD)
    This subpathway is part of the pathway ADP-L-glycero-beta-D-manno-heptose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate, the pathway ADP-L-glycero-beta-D-manno-heptose biosynthesis and in Nucleotide-sugar biosynthesis.

    Pathwayi: LPS core biosynthesis

    This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei7 – 71Nucleophile
    Metal bindingi7 – 71MagnesiumCombined sources1 Publication
    Binding sitei7 – 71Substrate1 Publication
    Active sitei9 – 91Proton donor
    Metal bindingi9 – 91Magnesium; via carbonyl oxygenCombined sources1 Publication
    Sitei50 – 501Stabilizes the phosphoryl groupBy similarity
    Binding sitei57 – 571Substrate1 Publication
    Metal bindingi89 – 891ZincCombined sources1 Publication
    Metal bindingi91 – 911Zinc; via pros nitrogenCombined sources1 Publication
    Metal bindingi97 – 971ZincCombined sources1 Publication
    Metal bindingi99 – 991ZincCombined sources1 Publication
    Binding sitei100 – 1001Substrate1 Publication
    Sitei100 – 1001Contributes to substrate recognitionBy similarity
    Sitei101 – 1011Stabilizes the phosphoryl groupBy similarity
    Metal bindingi126 – 1261MagnesiumCombined sources
    Binding sitei129 – 1291Substrate1 Publication

    GO - Molecular functioni

    • D,D-heptose 1,7-bisphosphate phosphatase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciBBRO257310:BB4091-MONOMER.
    BRENDAi3.1.3.82. 227.
    UniPathwayiUPA00356; UER00438.
    UPA00958.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (EC:3.1.3.82)
    Alternative name(s):
    D,D-heptose 1,7-bisphosphate phosphatase
    Short name:
    HBP phosphatase
    Gene namesi
    Ordered Locus Names:BB4091
    OrganismiBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
    Taxonomic identifieri257310 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
    Proteomesi
    • UP000001027 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 – 179179D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatasePRO_0000417695Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi257310.BB4091.

    Structurei

    Secondary structure

    1
    179
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64Combined sources
    Turni9 – 113Combined sources
    Helixi23 – 253Combined sources
    Helixi32 – 4110Combined sources
    Beta strandi45 – 517Combined sources
    Turni53 – 586Combined sources
    Helixi62 – 7817Combined sources
    Beta strandi85 – 895Combined sources
    Beta strandi98 – 1003Combined sources
    Helixi105 – 11410Combined sources
    Beta strandi122 – 1276Combined sources
    Helixi128 – 13710Combined sources
    Beta strandi140 – 1456Combined sources
    Turni146 – 1483Combined sources
    Helixi149 – 1557Combined sources
    Beta strandi162 – 1676Combined sources
    Helixi168 – 17710Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L8HX-ray1.68A/B/C/D1-179[»]
    ProteinModelPortaliQ7WG29.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7WG29.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 195Substrate binding
    Regioni50 – 534Substrate binding

    Sequence similaritiesi

    Belongs to the GmhB family.Curated

    Phylogenomic databases

    eggNOGiENOG4108ZI0. Bacteria.
    COG0241. LUCA.
    HOGENOMiHOG000016503.
    KOiK03273.
    OMAiDEWVALP.
    OrthoDBiPOG091H01YE.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR006549. HAD-SF_hydro_IIIA.
    IPR004446. Heptose_bisP_phosphatase.
    IPR006543. Histidinol-phos.
    [Graphical view]
    PIRSFiPIRSF004682. GmhB. 1 hit.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
    TIGR01656. Histidinol-ppas. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q7WG29-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLIILDRDG VVNQDSDAFV KSPDEWIALP GSLQAIARLT QADWTVVLAT
    60 70 80 90 100
    NQSGLARGLF DTATLNAIHD KMHRALAQMG GVVDAIFMCP HGPDDGCACR
    110 120 130 140 150
    KPLPGMYRDI ARRYDVDLAG VPAVGDSLRD LQAAAQAGCA PWLVQTGNGR
    160 170
    KTLAQGGLPE GTRVCEDLAA VAEQLLQEA
    Length:179
    Mass (Da):19,035
    Last modified:October 1, 2003 - v1
    Checksum:iB95E1F61A6B3F7AD
    GO

    Mass spectrometryi

    Molecular mass is 19034 Da from positions 1 - 179. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BX640449 Genomic DNA. Translation: CAE34454.1.
    RefSeqiWP_003814404.1. NC_002927.3.

    Genome annotation databases

    EnsemblBacteriaiCAE34454; CAE34454; BB4091.
    KEGGibbr:BB4091.
    PATRICi21141607. VBIBorBro124907_4158.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BX640449 Genomic DNA. Translation: CAE34454.1.
    RefSeqiWP_003814404.1. NC_002927.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L8HX-ray1.68A/B/C/D1-179[»]
    ProteinModelPortaliQ7WG29.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi257310.BB4091.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAE34454; CAE34454; BB4091.
    KEGGibbr:BB4091.
    PATRICi21141607. VBIBorBro124907_4158.

    Phylogenomic databases

    eggNOGiENOG4108ZI0. Bacteria.
    COG0241. LUCA.
    HOGENOMiHOG000016503.
    KOiK03273.
    OMAiDEWVALP.
    OrthoDBiPOG091H01YE.

    Enzyme and pathway databases

    UniPathwayiUPA00356; UER00438.
    UPA00958.
    BioCyciBBRO257310:BB4091-MONOMER.
    BRENDAi3.1.3.82. 227.

    Miscellaneous databases

    EvolutionaryTraceiQ7WG29.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR006549. HAD-SF_hydro_IIIA.
    IPR004446. Heptose_bisP_phosphatase.
    IPR006543. Histidinol-phos.
    [Graphical view]
    PIRSFiPIRSF004682. GmhB. 1 hit.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01662. HAD-SF-IIIA. 1 hit.
    TIGR01656. Histidinol-ppas. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGMHBB_BORBR
    AccessioniPrimary (citable) accession number: Q7WG29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2012
    Last sequence update: October 1, 2003
    Last modified: September 7, 2016
    This is version 91 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

    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.