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Entry version 141 (11 Dec 2019)
Sequence version 2 (27 Apr 2001)
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Protein

Beta-phosphoglucomutase

Gene

pgmB

Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
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

Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C1 anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.2 Publications

Miscellaneous

The catalysis proceeds via a phosphoenzyme formed by reaction of an active-site nucleophile with the cofactor glucose 1,6-diphosphate (G1,6-diP). The phosphorylated mutase binds either G1P or G6P and transfers the phosphoryl group to the C6OH or C1OH, respectively.

<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

Mg2+2 PublicationsNote: Binds 2 magnesium ions per subunit.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Competitively inhibited by alpha-D-galactose-1-phosphate.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

  1. KM=14.6 µM for beta-glucose 1-phosphate (at pH 7 and 25 degrees Celsius)2 Publications
  2. KM=20 µM for alpha-D-glucose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius)2 Publications
  3. KM=100 µM for alpha-D-fructose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius)2 Publications
  4. KM=270 µM for magnesium (at pH 7 and 25 degrees Celsius)2 Publications
  5. KM=800 µM for acetyl-phosphate (at pH 7 and 25 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is around 7. Relatively stable in solution within the pH range of 5-9.5.2 Publications

    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 sitei8Nucleophile1
    <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 bindingi8Magnesium 11
    Metal bindingi8Magnesium 21
    Active sitei10Proton donor1
    Metal bindingi10Magnesium 11
    Metal bindingi10Magnesium 2; via carbonyl oxygen1
    <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 sitei24Substrate1
    Binding sitei52Substrate1
    Binding sitei76Substrate1
    <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>Sitei114Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups1
    Binding sitei145Substrate1
    Sitei145Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups1
    Metal bindingi169Magnesium 11
    Metal bindingi170Magnesium 11
    Metal bindingi170Magnesium 21

    <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 functionIsomerase
    Biological processCarbohydrate metabolism
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    LLAC272623:L0001-MONOMER
    MetaCyc:MONOMER-5821

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    5.4.2.6 2903

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P71447

    <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:
    Beta-phosphoglucomutase (EC:5.4.2.6)
    Short name:
    Beta-PGM
    <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:pgmB
    Ordered Locus Names:LL0429
    ORF Names:L0001
    <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>OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
    <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 identifieri272623 [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 lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
    <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
    • UP000002196 <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

    <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

    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>Mutagenesisi8D → A: Inactive. 1 Publication1
    Mutagenesisi8D → E: Inactive. 1 Publication1
    Mutagenesisi10D → A: Inactive. 1 Publication1
    Mutagenesisi10D → E: Inactive. 1 Publication1
    Mutagenesisi10D → N: Inactive. 1 Publication1
    Mutagenesisi10D → S: Inactive. 1 Publication1
    Mutagenesisi16T → P: 500-fold reduction in the rate constant for Asp-8 phosphorylation by beta-G1,6bisP. 6,700-fold reduction in the apparent rate constant for cycling of the phosphorylated enzyme to convert beta-G1P to G6P. 13-fold increase in the estimated rate constant for phosphoryl transfer from the phospho-Asp8 to water. 1 Publication1
    Mutagenesisi20H → A: Impairs Asp-8 phosphorylation by beta-G1,6bisP and phosphoryl transfer from the phospho-Asp8 to the substrate beta-G1P. 1 Publication1
    Mutagenesisi20H → N: 300-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. 1 Publication1
    Mutagenesisi20H → Q: 8-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. 1 Publication1
    Mutagenesisi45K → A: 20'000-fold decrease in Kcat/KM. 1 Publication1
    Mutagenesisi46G → A: 1'000'000-fold decrease in Kcat/KM. 1 Publication1
    Mutagenesisi46G → P: 100'000-fold decrease in Kcat/KM. 1 Publication1
    Mutagenesisi46G → V: 10'000-fold decrease in Kcat/KM. 1 Publication1
    Mutagenesisi49R → K: 1'000'000-fold decrease in Kcat/KM. 1 Publication1
    Mutagenesisi52S → A: Wild-type activity. 1 Publication1
    Mutagenesisi76K → A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. 1 Publication1
    Mutagenesisi170D → A: Impaired, but active with an increase in the affinity for G1P. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB02317 Alpha-D-Galactose-1-Phosphate
    DB02835 Alpha-D-Glucose 1,6-Bisphosphate
    DB01857 Phosphoaspartate

    <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_00001080531 – 221Beta-phosphoglucomutaseAdd BLAST221

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei84-aspartylphosphate1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

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

    More...
    PaxDbi
    P71447

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By maltose, trehalose and sucrose and repressed by glucose and lactose.3 Publications

    <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.

    8 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    272623.L0001

    <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

    1221
    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
    P71447

    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
    P71447

    <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>Regioni8 – 10Substrate binding3
    Regioni44 – 49Substrate binding6
    Regioni114 – 118Substrate binding5

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4107URF Bacteria
    COG0637 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K01838

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    TQTAKVH

    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
    IPR010976 B-phosphoglucomutase_hydrolase
    IPR010972 Beta-phosphoglucomutase
    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
    TIGR01990 bPGM, 1 hit
    TIGR01509 HAD-SF-IA-v3, 1 hit
    TIGR02009 PGMB-YQAB-SF, 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.

    P71447-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MFKAVLFDLD GVITDTAEYH FRAWKALAEE IGINGVDRQF NEQLKGVSRE
    60 70 80 90 100
    DSLQKILDLA DKKVSAEEFK ELAKRKNDNY VKMIQDVSPA DVYPGILQLL
    110 120 130 140 150
    KDLRSNKIKI ALASASKNGP FLLEKMNLTG YFDAIADPAE VAASKPAPDI
    160 170 180 190 200
    FIAAAHAVGV APSESIGLED SQAGIQAIKD SGALPIGVGR PEDLGDDIVI
    210 220
    VPDTSYYTLE FLKEVWLQKQ K
    Length:221
    Mass (Da):24,209
    Last modified:April 27, 2001 - v2
    <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:i53AC0BF0FA249EFC
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti125K → R in CAA94734 (PubMed:9084169).Curated1
    Sequence conflicti206Y → H in CAA94734 (PubMed:9084169).Curated1

    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
    Z70730 Genomic DNA Translation: CAA94734.1
    AE005176 Genomic DNA Translation: AAK04527.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E86678

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_266585.1, NC_002662.1
    WP_010905331.1, NC_002662.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAK04527; AAK04527; L0001

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1114041

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    lla:L0001

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|272623.7.peg.467

    <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
    Z70730 Genomic DNA Translation: CAA94734.1
    AE005176 Genomic DNA Translation: AAK04527.1
    PIRiE86678
    RefSeqiNP_266585.1, NC_002662.1
    WP_010905331.1, NC_002662.1

    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
    1LVHX-ray2.30A/B1-221[»]
    1O03X-ray1.40A1-221[»]
    1O08X-ray1.20A1-221[»]
    1Z4NX-ray1.97A/B1-221[»]
    1Z4OX-ray1.90A/B1-221[»]
    1ZOLX-ray1.90A1-221[»]
    2WF5X-ray1.30A1-221[»]
    2WF6X-ray1.40A1-221[»]
    2WF7X-ray1.05A1-221[»]
    2WF8X-ray1.20A1-221[»]
    2WF9X-ray1.40A1-221[»]
    2WFAX-ray1.65A1-221[»]
    2WHEX-ray1.55A1-221[»]
    3FM9X-ray2.70A1-221[»]
    3ZI4X-ray1.33A1-221[»]
    4C4RX-ray1.10A1-221[»]
    4C4SX-ray1.50A1-221[»]
    4C4TX-ray1.50A1-221[»]
    5O6PX-ray2.20A1-221[»]
    5O6RX-ray1.36A1-221[»]
    5OJZX-ray1.30A1-220[»]
    5OK0X-ray2.15A1-218[»]
    5OK1X-ray1.86A1-218[»]
    5OK2X-ray1.10A1-218[»]
    5OLWX-ray2.28A/B1-221[»]
    5OLXX-ray1.38A1-221[»]
    5OLYX-ray2.00A/G1-221[»]
    SMRiP71447
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi272623.L0001

    Chemistry databases

    DrugBankiDB02317 Alpha-D-Galactose-1-Phosphate
    DB02835 Alpha-D-Glucose 1,6-Bisphosphate
    DB01857 Phosphoaspartate

    Proteomic databases

    PaxDbiP71447

    Genome annotation databases

    EnsemblBacteriaiAAK04527; AAK04527; L0001
    GeneIDi1114041
    KEGGilla:L0001
    PATRICifig|272623.7.peg.467

    Phylogenomic databases

    eggNOGiENOG4107URF Bacteria
    COG0637 LUCA
    KOiK01838
    OMAiTQTAKVH

    Enzyme and pathway databases

    BioCyciLLAC272623:L0001-MONOMER
    MetaCyc:MONOMER-5821
    BRENDAi5.4.2.6 2903
    SABIO-RKiP71447

    Miscellaneous databases

    EvolutionaryTraceiP71447

    Family and domain databases

    Gene3Di1.10.150.240, 1 hit
    3.40.50.1000, 1 hit
    InterProiView protein in InterPro
    IPR010976 B-phosphoglucomutase_hydrolase
    IPR010972 Beta-phosphoglucomutase
    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
    TIGRFAMsiTIGR01990 bPGM, 1 hit
    TIGR01509 HAD-SF-IA-v3, 1 hit
    TIGR02009 PGMB-YQAB-SF, 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 nameiPGMB_LACLA
    <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: P71447
    <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: July 15, 1998
    Last sequence update: April 27, 2001
    Last modified: December 11, 2019
    This is version 141 of the entry and version 2 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, Direct protein sequencing, 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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