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Entry version 150 (23 Feb 2022)
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%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+2 PublicationsNote: Binds 2 magnesium ions per subunit.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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)1 Publication
  2. KM=20 µM for alpha-D-glucose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius)1 Publication
  3. KM=100 µM for alpha-D-fructose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius)1 Publication
  4. KM=270 µM for magnesium (at pH 7 and 25 degrees Celsius)1 Publication
  5. KM=800 µM for acetyl-phosphate (at pH 7 and 25 degrees Celsius)1 Publication

pH dependencei

Optimum pH is around 7. Relatively stable in solution within the pH range of 5-9.5.1 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 sitei8Nucleophile1
<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 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%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 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

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%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:
Beta-phosphoglucomutase1 Publication (EC:5.4.2.63 Publications)
Short name:
Beta-PGM1 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:pgmB1 Publication
Ordered Locus Names:LL0429
ORF Names:L0001
<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>OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
<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 identifieri272623 [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 lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
<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
  • UP000002196 <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

<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

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%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>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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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%5Fsection">'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%5Fsection">'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

Biological Magnetic Resonance Data Bank

More...
BMRBi
P71447

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
COG0637, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_045011_13_3_9

Identification of Orthologs from Complete Genome Data

More...
OMAi
TQTAKVH

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02598, HAD_BPGM, 1 hit

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%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.

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

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[»]
6H8UX-ray1.90A1-221[»]
6H8VX-ray1.84A/B1-221[»]
6H8WX-ray1.98A1-221[»]
6H8XX-ray1.83A/B1-221[»]
6H8YX-ray1.89A1-221[»]
6H8ZX-ray1.60A1-221[»]
6H90X-ray1.31A1-221[»]
6H91X-ray2.38A/B1-221[»]
6H92X-ray2.60A/B1-221[»]
6H93X-ray1.77A/B1-221[»]
6H94X-ray1.49A1-221[»]
6HDFX-ray1.40A/B1-221[»]
6HDGX-ray1.15A1-221[»]
6HDHX-ray1.62A/B1-221[»]
6HDIX-ray2.03A/B1-221[»]
6HDJX-ray1.16A1-221[»]
6HDKX-ray1.24A1-221[»]
6HDLX-ray1.16A1-221[»]
6HDMX-ray1.30A1-221[»]
6I03X-ray1.02A1-221[»]
6QZGX-ray2.47A/B1-221[»]
6YDJX-ray1.04A1-221[»]
6YDKX-ray2.02A1-221[»]
6YDLX-ray1.52A1-221[»]
6YDMX-ray2.10A/B1-221[»]
BMRBiP71447
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
KEGGilla:L0001
PATRICifig|272623.7.peg.467

Phylogenomic databases

eggNOGiCOG0637, Bacteria
HOGENOMiCLU_045011_13_3_9
OMAiTQTAKVH

Enzyme and pathway databases

BRENDAi5.4.2.6, 2903
SABIO-RKiP71447

Miscellaneous databases

EvolutionaryTraceiP71447

Family and domain databases

CDDicd02598, HAD_BPGM, 1 hit
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

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%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: April 27, 2001
Last modified: February 23, 2022
This is version 150 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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