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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Active sitei7Nucleophile1
    Metal bindingi7MagnesiumCombined sources1 Publication1
    Binding sitei7Substrate1 Publication1
    Active sitei9Proton donor1
    Metal bindingi9Magnesium; via carbonyl oxygenCombined sources1 Publication1
    Sitei50Stabilizes the phosphoryl groupBy similarity1
    Binding sitei57Substrate1 Publication1
    Metal bindingi89ZincCombined sources1 Publication1
    Metal bindingi91Zinc; via pros nitrogenCombined sources1 Publication1
    Metal bindingi97ZincCombined sources1 Publication1
    Metal bindingi99ZincCombined sources1 Publication1
    Binding sitei100Substrate1 Publication1
    Sitei100Contributes to substrate recognitionBy similarity1
    Sitei101Stabilizes the phosphoryl groupBy similarity1
    Metal bindingi126MagnesiumCombined sources1
    Binding sitei129Substrate1 Publication1

    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

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00004176951 – 179D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphataseAdd BLAST179

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi257310.BB4091.

    Structurei

    Secondary structure

    1179
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 6Combined sources4
    Turni9 – 11Combined sources3
    Helixi23 – 25Combined sources3
    Helixi32 – 41Combined sources10
    Beta strandi45 – 51Combined sources7
    Turni53 – 58Combined sources6
    Helixi62 – 78Combined sources17
    Beta strandi85 – 89Combined sources5
    Beta strandi98 – 100Combined sources3
    Helixi105 – 114Combined sources10
    Beta strandi122 – 127Combined sources6
    Helixi128 – 137Combined sources10
    Beta strandi140 – 145Combined sources6
    Turni146 – 148Combined sources3
    Helixi149 – 155Combined sources7
    Beta strandi162 – 167Combined sources6
    Helixi168 – 177Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3L8HX-ray1.68A/B/C/D1-179[»]
    ProteinModelPortaliQ7WG29.
    SMRiQ7WG29.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7WG29.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni15 – 19Substrate binding5
    Regioni50 – 53Substrate binding4

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3L8HX-ray1.68A/B/C/D1-179[»]
    ProteinModelPortaliQ7WG29.
    SMRiQ7WG29.
    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.
    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: November 2, 2016
    This is version 92 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.