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UniProtKB - P77247 (HXPB_ECOLI)

Entry version 158 (23 Feb 2022)
Sequence version 1 (01 Feb 1997)
Previous versions | rss
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Protein

Hexitol phosphatase B

Gene

hxpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sugar-phosphate phosphohydrolase that catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate (PubMed:27941785).

Also catalyzes the dephosphorylation of 2-deoxyglucose 6-phosphate (2dGlu6P); this is a biologically important activity in vivo since it contributes to the elimination of this toxic compound and plays an important role in the resistance of E.coli to 2-deoxyglucose (PubMed:16990279).

To a lesser extent, is also able to dephosphorylate mannose 6-phosphate (Man6P), erythrose-4-phosphate, 2-deoxyribose-5-phosphate (2dRib5P), ribose-5-phosphate (Rib5P) and glucose-6-phosphate (Glu6P) in vitro (PubMed:16990279).

3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 Publication, Zn2+1 PublicationNote: Requires the presence of a divalent metal cation for activity. Can use zinc, manganese, cobalt or magnesium.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 33 sec(-1) with 2-deoxyglucose-6-P as substrate. kcat is 11 sec(-1) with mannose-6-P as substrate. kcat is 9.4 sec(-1) with 2-deoxyribose-5-P as substrate. kcat is 2.8 sec(-1) with ribose-5-P as substrate. kcat is 25 sec(-1) with glucose-6-P as substrate.1 Publication
  1. KM=0.61 mM for 2-deoxyglucose-6-P (with manganese ions as cofactor and at pH 9)1 Publication
  2. KM=2.5 mM for 2-deoxyribose-5-P (with zinc ions as cofactor and at pH 9)1 Publication
  3. KM=2.6 mM for ribose-5-P (with zinc ions as cofactor and at pH 9)1 Publication
  4. KM=3.6 mM for glucose-6-P (with zinc ions as cofactor and at pH 9)1 Publication
  5. KM=4.7 mM for mannose-6-P (with zinc 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei13NucleophileBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi13Divalent metal cation1 Publication1
Active sitei15Proton donorBy similarity1
Metal bindingi15Divalent metal cation; via carbonyl oxygen1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei148Substrate1 Publication1
Metal bindingi173Divalent metal cation1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:G6932-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Hexitol phosphatase B1 Publication
Alternative name(s):
2-deoxyglucose-6-phosphate phosphatase1 Publication (EC:3.1.3.681 Publication)
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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:hxpB1 Publication
Synonyms:yniCImported
Ordered Locus Names:b1727, JW1716
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene are much more sensitive to the presence of 2-deoxyglucose in the growth medium than wild-type.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi13D → A: Loss of phosphatase activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001080611 – 222Hexitol phosphatase BAdd BLAST222

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P77247

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P77247

PRoteomics IDEntifications database

More...PRIDEi		P77247

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P77247

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4263414, 9 interactors

Database of interacting proteins

More...DIPi		DIP-12777N

Protein interaction database and analysis system

More...IntActi		P77247, 8 interactors

STRING: functional protein association networks

More...STRINGi		511145.b1727

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P77247

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P77247

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni13 – 15Substrate binding1 Publication3
Regioni115 – 116Substrate binding1 Publication2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0637, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_045011_13_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P77247

Database for complete collections of gene phylogenies

More...PhylomeDBi		P77247

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.150.240, 1 hit
3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036412, HAD-like_sf
IPR006439, HAD-SF_hydro_IA
IPR041492, HAD_2
IPR023214, HAD_sf
IPR023198, PGP-like_dom2

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13419, HAD_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00413, HADHALOGNASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56784, SSF56784, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01509, HAD-SF-IA-v3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P77247-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTPRQILAA IFDMDGLLID SEPLWDRAEL DVMASLGVDI SRRNELPDTL 
        60         70         80         90        100
GLRIDMVVDL WYARQPWNGP SRQEVVERVI ARAISLVEET RPLLPGVREA 
       110        120        130        140        150
VALCKEQGLL VGLASASPLH MLEKVLTMFD LRDSFDALAS AEKLPYSKPH 
       160        170        180        190        200
PQVYLDCAAK LGVDPLTCVA LEDSVNGMIA SKAARMRSIV VPAPEAQNDP 
       210        220 
RFVLADVKLS SLTELTAKDL LG
Length:222
Mass (Da):24,330
Last modified:February 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i76FE1F2A331476A7
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74797.1
AP009048 Genomic DNA Translation: BAA15508.1

Protein sequence database of the Protein Information Resource

More...PIRi		G64931

NCBI Reference Sequences

More...RefSeqi		NP_416241.1, NC_000913.3
WP_000106833.1, NZ_SSZK01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74797; AAC74797; b1727
BAA15508; BAA15508; BAA15508

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945632

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1716
eco:b1727

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.529

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74797.1
AP009048 Genomic DNA Translation: BAA15508.1
PIRiG64931
RefSeqiNP_416241.1, NC_000913.3
WP_000106833.1, NZ_SSZK01000001.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TE2X-ray1.76A/B1-222[»]
SMRiP77247
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263414, 9 interactors
DIPiDIP-12777N
IntActiP77247, 8 interactors
STRINGi511145.b1727

2D gel databases

SWISS-2DPAGEiP77247

Proteomic databases

jPOSTiP77247
PaxDbiP77247
PRIDEiP77247

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		945632

Genome annotation databases

EnsemblBacteriaiAAC74797; AAC74797; b1727
BAA15508; BAA15508; BAA15508
GeneIDi945632
KEGGiecj:JW1716
eco:b1727
PATRICifig|1411691.4.peg.529

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB3744

Phylogenomic databases

eggNOGiCOG0637, Bacteria
HOGENOMiCLU_045011_13_1_6
InParanoidiP77247
PhylomeDBiP77247

Enzyme and pathway databases

BioCyciEcoCyc:G6932-MONOMER

Miscellaneous databases

EvolutionaryTraceiP77247

Protein Ontology

More...PROi		PR:P77247

Family and domain databases

Gene3Di1.10.150.240, 1 hit
3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR036412, HAD-like_sf
IPR006439, HAD-SF_hydro_IA
IPR041492, HAD_2
IPR023214, HAD_sf
IPR023198, PGP-like_dom2
PfamiView protein in Pfam
PF13419, HAD_2, 1 hit
PRINTSiPR00413, HADHALOGNASE
SUPFAMiSSF56784, SSF56784, 1 hit
TIGRFAMsiTIGR01509, HAD-SF-IA-v3, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHXPB_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P77247
Secondary accession number(s): P78167
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: February 23, 2022
This is version 158 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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