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Protein

Hexitol phosphatase A

Gene

hxpA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sugar-phosphate phosphohydrolase that appears to contribute to butanol tolerance (PubMed:27941785). Catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate (PubMed:27941785). Is also able to dephosphorylate other sugar phosphates in vitro including ribose-5-phosphate (Rib5P), 2-deoxyribose-5-phosphate, fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), and glucose-6-phosphate (Glu6P) (PubMed:16990279). Selectively hydrolyzes beta-D-glucose-1-phosphate (bGlu1P) and has no activity with the alpha form (PubMed:16990279).3 Publications

Catalytic activityi

Sugar phosphate + H2O = sugar + phosphate.1 Publication
D-mannitol 1-phosphate + H2O = D-mannitol + phosphate.1 Publication
Sorbitol 6-phosphate + H2O = sorbitol + phosphate.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 PublicationNote: Requires the presence of a divalent metal cation for activity. Can use magnesium, manganese or cobalt.1 Publication

Kineticsi

kcat is 3.7 sec(-1) with fructose-1-P as substrate. kcat is 2.7 sec(-1) with ribose-5-P as substrate. kcat is 13 sec(-1) with glucose-6-P as substrate. kcat is 3.1 sec(-1) with fructose-6-P as substrate. kcat is 7.5 sec(-1) with beta-D-glucose-1-P as substrate.1 Publication
  1. KM=1.0 mM for fructose-1-P (with magnesium ions as cofactor and at pH 9)1 Publication
  2. KM=1.3 mM for fructose-6-P (with magnesium ions as cofactor and at pH 9)1 Publication
  3. KM=1.8 mM for glucose-6-P (with cobalt ions as cofactor and at pH 9)1 Publication
  4. KM=2.2 mM for ribose-5-P (with magnesium ions as cofactor and at pH 9)1 Publication
  5. KM=7.0 mM for beta-D-glucose-1-P (with manganese ions as cofactor and at pH 9)1 Publication

    pH dependencei

    Optimum pH is between 6 and 7.5.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei9NucleophileBy similarity1
    Metal bindingi9Divalent metal cationBy similarity1
    Active sitei11Proton donorBy similarity1
    Metal bindingi11Divalent metal cation; via carbonyl oxygenBy similarity1
    Binding sitei138SubstrateBy similarity1
    Metal bindingi163Divalent metal cationBy similarity1

    GO - Molecular functioni

    • cobalt ion binding Source: UniProtKB
    • glycerol-3-phosphatase activity Source: EcoCyc
    • magnesium ion binding Source: UniProtKB
    • manganese ion binding Source: UniProtKB
    • mannitol-1-phosphatase activity Source: EcoCyc
    • sorbitol-6-phosphatase activity Source: EcoCyc
    • sugar-phosphatase activity Source: UniProtKB

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase
    Biological processCarbohydrate metabolism
    LigandCobalt, Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G7187-MONOMER.
    MetaCyc:G7187-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hexitol phosphatase A1 Publication
    Alternative name(s):
    Mannitol-1-phosphatase1 Publication (EC:3.1.3.221 Publication)
    Sorbitol-6-phosphatase1 Publication (EC:3.1.3.501 Publication)
    Sugar-phosphatase1 Publication (EC:3.1.3.231 Publication)
    Gene namesi
    Name:hxpA1 Publication
    Synonyms:yfbTImported
    Ordered Locus Names:b2293, JW5376
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14104. yfbT.

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show a reduced growth rate at high butanol concentrations compared to wild-type. They also show a consistent change in the level of mannitol, D-sorbitol, galactitol, L-tyrosine, 3-amino-3-(4-hydroxyphenyl)propanoate and N-hydroxy-L-phenylalanine.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001080591 – 216Hexitol phosphatase AAdd BLAST216

    Proteomic databases

    PaxDbiP77625.
    PRIDEiP77625.

    Interactioni

    Protein-protein interaction databases

    BioGridi4262967. 8 interactors.
    DIPiDIP-11972N.
    IntActiP77625. 2 interactors.
    MINTiMINT-1275778.
    STRINGi316385.ECDH10B_2455.

    Structurei

    3D structure databases

    ProteinModelPortaliP77625.
    SMRiP77625.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni9 – 11Substrate bindingBy similarity3
    Regioni106 – 107Substrate bindingBy similarity2

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105EVE. Bacteria.
    COG0637. LUCA.
    HOGENOMiHOG000248341.
    InParanoidiP77625.
    KOiK19270.
    PhylomeDBiP77625.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiView protein in InterPro
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    PfamiView protein in Pfam
    PF13419. HAD_2. 1 hit.
    PRINTSiPR00413. HADHALOGNASE.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01549. HAD-SF-IA-v1. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P77625-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRCKGFLFDL DGTLVDSLPA VERAWSNWAR RHGLAPEEVL AFIHGKQAIT
    60 70 80 90 100
    SLRHFMAGKS EADIAAEFTR LEHIEATETE GITALPGAIA LLSHLNKAGI
    110 120 130 140 150
    PWAIVTSGSM PVARARHKIA GLPAPEVFVT AERVKRGKPE PDAYLLGAQL
    160 170 180 190 200
    LGLAPQECVV VEDAPAGVLS GLAAGCHVIA VNAPADTPRL NEVDLVLHSL
    210
    EQITVTKQPN GDVIIQ
    Length:216
    Mass (Da):23,008
    Last modified:September 26, 2001 - v2
    Checksum:iC687DF877E2706EF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75353.2.
    AP009048 Genomic DNA. Translation: BAA16129.2.
    PIRiC65001.
    RefSeqiNP_416796.2. NC_000913.3.
    WP_001203392.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75353; AAC75353; b2293.
    BAA16129; BAA16129; BAA16129.
    GeneIDi946777.
    KEGGiecj:JW5376.
    eco:b2293.
    PATRICifig|511145.12.peg.2387.

    Similar proteinsi

    Entry informationi

    Entry nameiHXPA_ECOLI
    AccessioniPrimary (citable) accession number: P77625
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: September 26, 2001
    Last modified: August 30, 2017
    This is version 132 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families