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P46452

- GMHBB_HAEIN

UniProt

P46452 - GMHBB_HAEIN

Protein

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

Gene

gmhB

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.By similarity

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity
    Zinc.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei8 – 81NucleophileBy similarity
    Metal bindingi8 – 81MagnesiumBy similarity
    Active sitei10 – 101Proton donorBy similarity
    Metal bindingi10 – 101Magnesium; via carbonyl oxygenBy similarity
    Sitei50 – 501Stabilizes the phosphoryl groupBy similarity
    Metal bindingi89 – 891ZincBy similarity
    Metal bindingi91 – 911Zinc; via amide nitrogenBy similarity
    Metal bindingi103 – 1031ZincBy similarity
    Metal bindingi105 – 1051ZincBy similarity
    Sitei106 – 1061Contributes to substrate recognitionBy similarity
    Sitei107 – 1071Stabilizes the phosphoryl groupBy similarity
    Metal bindingi132 – 1321MagnesiumBy similarity
    Metal bindingi133 – 1331MagnesiumBy similarity
    Binding sitei133 – 1331SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. ADP-L-glycero-beta-D-manno-heptose biosynthetic process Source: UniProtKB-UniPathway
    2. carbohydrate metabolic process Source: UniProtKB-KW
    3. dephosphorylation Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00356; UER00438.
    UPA00976.

    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
    Name:gmhB
    Ordered Locus Names:HI_0621.1
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 184184D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatasePRO_0000209392Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi71421.HI0621.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP46452.
    SMRiP46452. Positions 4-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni8 – 103Substrate bindingBy similarity
    Regioni16 – 194Substrate bindingBy similarity
    Regioni50 – 534Substrate bindingBy similarity
    Regioni106 – 1072Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the GmhB family.Curated

    Phylogenomic databases

    eggNOGiCOG0241.
    KOiK03273.
    OMAiFMQLTEW.
    OrthoDBiEOG6QG8GT.
    PhylomeDBiP46452.

    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.
    TIGRFAMsiTIGR00213. GmhB_yaeD. 1 hit.
    TIGR01662. HAD-SF-IIIA. 1 hit.
    TIGR01656. Histidinol-ppas. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P46452-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKAIFLDRD GTLNIDYGYV HEIDNFKFID GVIDALRELK KMGYMLVLVT    50
    NQSGIARGYF SEDQFLQLTE WMDWSLAEQD VDLDGIYYCP HHSEGKGEYK 100
    EDCDCRKPKS GMLLQAIKEL KIDPTQSIMV GDKVEDLKAG IGAKVKMNVL 150
    VRTGKPVTGE GEGIADYVLD SIVDLPRILK RLKK 184
    Length:184
    Mass (Da):20,810
    Last modified:November 1, 1995 - v1
    Checksum:i49D1D56DA6DF3DBD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC22281.1.
    RefSeqiNP_438781.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC22281; AAC22281; HI_0621.1.
    GeneIDi949688.
    KEGGihin:HI0621.1.
    PATRICi20189829. VBIHaeInf48452_0647.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC22281.1 .
    RefSeqi NP_438781.1. NC_000907.1.

    3D structure databases

    ProteinModelPortali P46452.
    SMRi P46452. Positions 4-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI0621.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC22281 ; AAC22281 ; HI_0621.1 .
    GeneIDi 949688.
    KEGGi hin:HI0621.1.
    PATRICi 20189829. VBIHaeInf48452_0647.

    Phylogenomic databases

    eggNOGi COG0241.
    KOi K03273.
    OMAi FMQLTEW.
    OrthoDBi EOG6QG8GT.
    PhylomeDBi P46452.

    Enzyme and pathway databases

    UniPathwayi UPA00356 ; UER00438 .
    UPA00976 .

    Family and domain databases

    Gene3Di 3.40.50.1000. 1 hit.
    InterProi IPR023214. HAD-like_dom.
    IPR006549. HAD-SF_hydro_IIIA.
    IPR004446. Heptose_bisP_phosphatase.
    IPR006543. Histidinol-phos.
    [Graphical view ]
    PIRSFi PIRSF004682. GmhB. 1 hit.
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR00213. GmhB_yaeD. 1 hit.
    TIGR01662. HAD-SF-IIIA. 1 hit.
    TIGR01656. Histidinol-ppas. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
    2. Koonin E.V., Rudd K.E.
      Submitted (SEP-1995) to UniProtKB
      Cited for: IDENTIFICATION.
    3. "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides."
      Valvano M.A., Messner P., Kosma P.
      Microbiology 148:1979-1989(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.

    Entry informationi

    Entry nameiGMHBB_HAEIN
    AccessioniPrimary (citable) accession number: P46452
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 93 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

    Complete proteome, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3