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Entry version 123 (13 Nov 2019)
Sequence version 1 (27 Sep 2004)
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Protein

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

Gene

gmhB

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

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.3 Publications

Miscellaneous

Phosphatase activity is essential for nucleotide activation (fourth step). Zinc ion does not directly participate in catalysis, but probably functions to stabilize the loop conformation.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Protein has several cofactor binding sites:

<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 35.7 sec(-1) and 4.6 sec(-1) with beta-HBP and alpha-HBP as substrate, respectively. Thus, the enzyme displays 100-fold more efficiency towards the beta- than the alpha-anomer (PubMed:20050615). kcat is 0.51 sec(-1) and 0.039 sec(-1) with sedoheptulose-1,7-bisphosphate and fructose-1,6-bisphosphate as substrate, respectively (PubMed:20050615).1 Publication
  1. KM=5 µM for beta-HBP (at pH 7.5 and 25 degrees Celsius)3 Publications
  2. KM=67 µM for alpha-HBP (at pH 7.5 and 25 degrees Celsius)3 Publications
  3. KM=0.20 mM for HBP (at pH 8)3 Publications
  4. KM=0.42 mM for fructose-1,6-bisphosphate (at pH 9)3 Publications
  5. KM=610 µM for sedoheptulose-1,7-bisphosphate (at pH 7.5)3 Publications
  6. KM=1501 µM for fructose-1,6-bisphosphate (at pH 7.5)3 Publications

    pH dependencei

    Optimum pH is between 6 and 7.5.2 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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.3 Publications
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Bifunctional protein HldE (hldE), Bifunctional protein HldE (hldE)
    2. D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (gmhB)
    3. Bifunctional protein HldE (hldE), Bifunctional protein HldE (hldE)
    4. ADP-L-glycero-D-manno-heptose-6-epimerase (hldD), ADP-L-glycero-D-manno-heptose-6-epimerase (rfaD), ADP-L-glycero-D-manno-heptose-6-epimerase (rfaD), ADP-L-glycero-D-manno-heptose-6-epimerase (rfaD)
    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.2 Publications
    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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei11Nucleophile1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi11Magnesium1 Publication1
    Active sitei13Proton donor2 Publications1
    Metal bindingi13Magnesium; via carbonyl oxygen1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei53Stabilizes the phosphoryl group2 Publications1
    Metal bindingi92Zinc1 Publication1
    Metal bindingi94Zinc; via pros nitrogen1 Publication1
    Metal bindingi107Zinc1 Publication1
    Metal bindingi109Zinc1 Publication1
    Sitei110Contributes to substrate recognition1 Publication1
    Sitei111Stabilizes the phosphoryl group1 Publication1
    Metal bindingi136Magnesium1 Publication1
    Metal bindingi137Magnesium1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei137Substrate1 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

    GO - Biological processi

    <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, Lipopolysaccharide biosynthesis
    LigandMagnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:EG11736-MONOMER
    ECOL316407:JW0196-MONOMER
    MetaCyc:EG11736-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.3.82 2026

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00356;UER00438
    UPA00958

    <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_and_taxonomy_section">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:
    D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (EC:3.1.3.824 Publications)
    Alternative name(s):
    D,D-heptose 1,7-bisphosphate phosphatase
    Short name:
    HBP phosphatase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:gmhB
    Synonyms:yaeD
    Ordered Locus Names:b0200, JW0196
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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 result in the formation of an altered LPS core, but does not appear to disrupt full-length LPS production to an extent that the outer membrane permeability barrier is compromised.2 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi11D → N: Inactive. 1 Publication1
    Mutagenesisi13D → A: Inactive. 2 Publications1
    Mutagenesisi13D → N: Inactive. 2 Publications1
    Mutagenesisi92C → A: Reduces the catalytic efficiencies towards the alpha and beta-anomers of HBP. 1 Publication1
    Mutagenesisi107C → A: More than 3-fold reduction in the affinity binding of HBP. Reduces the catalytic efficiencies towards the alpha and beta-anomers of HBP. 2 Publications1
    Mutagenesisi109C → A: Reduces the catalytic efficiencies towards the alpha and beta-anomers of HBP. 1 Publication1
    Mutagenesisi110R → A: Significant reduction in the catalytic efficiency of hydrolysis of the physiological substrate HBP. 1 Publication1
    Mutagenesisi111K → N: Inactive. 1 Publication1
    Mutagenesisi137K → A: 8-fold reduction in the affinity binding of HBP. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002093891 – 191D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphataseAdd BLAST191

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P63228

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

    More...
    PaxDbi
    P63228

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P63228

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259752, 286 interactors
    849279, 4 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-47998N

    Protein interaction database and analysis system

    More...
    IntActi
    P63228, 11 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0200

    <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

    1191
    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
    P63228

    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
    P63228

    <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>Regioni11 – 13Substrate binding2 Publications3
    Regioni19 – 22Substrate binding1 Publication4
    Regioni53 – 56Substrate binding2 Publications4
    Regioni110 – 111Substrate 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 GmhB family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108ZI0 Bacteria
    COG0241 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000016501

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P63228

    KEGG Orthology (KO)

    More...
    KOi
    K03273

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P63228

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    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
    IPR006549 HAD-SF_hydro_IIIA
    IPR023214 HAD_sf
    IPR004446 Heptose_bisP_phosphatase
    IPR006543 Histidinol-phos

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR42891 PTHR42891, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF004682 GmhB, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56784 SSF56784, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00213 GmhB_yaeD, 1 hit
    TIGR01662 HAD-SF-IIIA, 1 hit
    TIGR01656 Histidinol-ppas, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P63228-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV
    60 70 80 90 100
    VVTNQSGIAR GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV
    110 120 130 140 150
    EEFRQVCDCR KPHPGMLLSA RDYLHIDMAA SYMVGDKLED MQAAVAANVG
    160 170 180 190
    TKVLVRTGKP ITPEAENAAD WVLNSLADLP QAIKKQQKPA Q
    Length:191
    Mass (Da):21,294
    Last modified:September 27, 2004 - 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:iE7814B34A23128FA
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence BAA03661 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    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
    D15061 Genomic DNA Translation: BAA03661.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73311.1
    AP009048 Genomic DNA Translation: BAA77877.1
    U70214 Genomic DNA Translation: AAB08628.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    H64744

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_414742.1, NC_000913.3
    WP_001140187.1, NZ_STEB01000032.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73311; AAC73311; b0200
    BAA77877; BAA77877; BAA77877

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    944879

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0196
    eco:b0200

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2078

    <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
    D15061 Genomic DNA Translation: BAA03661.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73311.1
    AP009048 Genomic DNA Translation: BAA77877.1
    U70214 Genomic DNA Translation: AAB08628.1
    PIRiH64744
    RefSeqiNP_414742.1, NC_000913.3
    WP_001140187.1, NZ_STEB01000032.1

    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
    2GMWX-ray1.50A/B1-191[»]
    3ESQX-ray1.70A1-191[»]
    3ESRX-ray1.95A1-191[»]
    3L1UX-ray1.95A/B1-191[»]
    3L1VX-ray1.95A/B1-191[»]
    3L8EX-ray1.64A/B1-187[»]
    3L8FX-ray1.79A1-187[»]
    3L8GX-ray2.18A1-187[»]
    SMRiP63228
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4259752, 286 interactors
    849279, 4 interactors
    DIPiDIP-47998N
    IntActiP63228, 11 interactors
    STRINGi511145.b0200

    Proteomic databases

    jPOSTiP63228
    PaxDbiP63228
    PRIDEiP63228

    Genome annotation databases

    EnsemblBacteriaiAAC73311; AAC73311; b0200
    BAA77877; BAA77877; BAA77877
    GeneIDi944879
    KEGGiecj:JW0196
    eco:b0200
    PATRICifig|1411691.4.peg.2078

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1687

    Phylogenomic databases

    eggNOGiENOG4108ZI0 Bacteria
    COG0241 LUCA
    HOGENOMiHOG000016501
    InParanoidiP63228
    KOiK03273
    PhylomeDBiP63228

    Enzyme and pathway databases

    UniPathwayiUPA00356;UER00438
    UPA00958
    BioCyciEcoCyc:EG11736-MONOMER
    ECOL316407:JW0196-MONOMER
    MetaCyc:EG11736-MONOMER
    BRENDAi3.1.3.82 2026

    Miscellaneous databases

    EvolutionaryTraceiP63228

    Protein Ontology

    More...
    PROi
    PR:P63228

    Family and domain databases

    Gene3Di3.40.50.1000, 1 hit
    InterProiView protein in InterPro
    IPR036412 HAD-like_sf
    IPR006549 HAD-SF_hydro_IIIA
    IPR023214 HAD_sf
    IPR004446 Heptose_bisP_phosphatase
    IPR006543 Histidinol-phos
    PANTHERiPTHR42891 PTHR42891, 1 hit
    PIRSFiPIRSF004682 GmhB, 1 hit
    SUPFAMiSSF56784 SSF56784, 1 hit
    TIGRFAMsiTIGR00213 GmhB_yaeD, 1 hit
    TIGR01662 HAD-SF-IIIA, 1 hit
    TIGR01656 Histidinol-ppas, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiGMHBB_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: P63228
    Secondary accession number(s): P31546
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: September 27, 2004
    Last modified: November 13, 2019
    This is version 123 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, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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