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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-Experimental evidence at protein leveli

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

Catalytic activityi

Beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate.

Cofactori

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

Enzyme regulationi

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

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
    Active sitei8Nucleophile1
    Metal bindingi8Magnesium 11
    Metal bindingi8Magnesium 21
    Active sitei10Proton donor1
    Metal bindingi10Magnesium 11
    Metal bindingi10Magnesium 2; via carbonyl oxygen1
    Binding sitei24Substrate1
    Binding sitei52Substrate1
    Binding sitei76Substrate1
    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

    GO - Molecular functioni

    • beta-phosphoglucomutase activity Source: UniProtKB
    • hydrolase activity Source: InterPro
    • magnesium ion binding Source: UniProtKB

    GO - Biological processi

    • carbohydrate metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-5821.
    BRENDAi5.4.2.6. 2903.
    SABIO-RKP71447.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-phosphoglucomutase (EC:5.4.2.6)
    Short name:
    Beta-PGM
    Gene namesi
    Name:pgmB
    Ordered Locus Names:LL0429
    ORF Names:L0001
    OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
    Taxonomic identifieri272623 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
    Proteomesi
    • UP000002196 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001080531 – 221Beta-phosphoglucomutaseAdd BLAST221

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei84-aspartylphosphate1 Publication1

    Post-translational modificationi

    Autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP71447.

    Expressioni

    Inductioni

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

    Interactioni

    Subunit structurei

    Monomer.8 Publications

    Protein-protein interaction databases

    STRINGi272623.L0001.

    Structurei

    Secondary structure

    1221
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 7Combined sources4
    Turni10 – 12Combined sources3
    Beta strandi13 – 15Combined sources3
    Helixi16 – 30Combined sources15
    Helixi38 – 41Combined sources4
    Turni42 – 46Combined sources5
    Helixi49 – 59Combined sources11
    Beta strandi60 – 62Combined sources3
    Helixi66 – 83Combined sources18
    Helixi84 – 86Combined sources3
    Helixi89 – 91Combined sources3
    Helixi96 – 105Combined sources10
    Beta strandi109 – 112Combined sources4
    Helixi119 – 125Combined sources7
    Helixi129 – 131Combined sources3
    Beta strandi133 – 135Combined sources3
    Turni138 – 140Combined sources3
    Beta strandi141 – 143Combined sources3
    Helixi149 – 157Combined sources9
    Helixi162 – 164Combined sources3
    Beta strandi165 – 171Combined sources7
    Helixi172 – 181Combined sources10
    Beta strandi184 – 189Combined sources6
    Helixi191 – 194Combined sources4
    Beta strandi196 – 203Combined sources8
    Helixi204 – 206Combined sources3
    Helixi209 – 217Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP71447.
    SMRiP71447.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP71447.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni8 – 10Substrate binding3
    Regioni44 – 49Substrate binding6
    Regioni114 – 118Substrate binding5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4107URF. Bacteria.
    COG0637. LUCA.
    KOiK01838.
    OMAiKYHYLAW.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR010976. B-phosphoglucomutase_hydrolase.
    IPR010972. Beta-phosphoglucomutase.
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    [Graphical view]
    PfamiPF13419. HAD_2. 1 hit.
    [Graphical view]
    PRINTSiPR00413. HADHALOGNASE.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01990. bPGM. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.
    TIGR02009. PGMB-YQAB-SF. 1 hit.

    Sequencei

    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
    Checksum:i53AC0BF0FA249EFC
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti125K → R in CAA94734 (PubMed:9084169).Curated1
    Sequence conflicti206Y → H in CAA94734 (PubMed:9084169).Curated1

    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.

    Genome annotation databases

    EnsemblBacteriaiAAK04527; AAK04527; L0001.
    GeneIDi1114041.
    KEGGilla:L0001.
    PATRICi22293074. VBILacLac136773_0467.

    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:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP71447.
    SMRiP71447.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272623.L0001.

    Proteomic databases

    PaxDbiP71447.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK04527; AAK04527; L0001.
    GeneIDi1114041.
    KEGGilla:L0001.
    PATRICi22293074. VBILacLac136773_0467.

    Phylogenomic databases

    eggNOGiENOG4107URF. Bacteria.
    COG0637. LUCA.
    KOiK01838.
    OMAiKYHYLAW.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-5821.
    BRENDAi5.4.2.6. 2903.
    SABIO-RKP71447.

    Miscellaneous databases

    EvolutionaryTraceiP71447.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR010976. B-phosphoglucomutase_hydrolase.
    IPR010972. Beta-phosphoglucomutase.
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    [Graphical view]
    PfamiPF13419. HAD_2. 1 hit.
    [Graphical view]
    PRINTSiPR00413. HADHALOGNASE.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01990. bPGM. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.
    TIGR02009. PGMB-YQAB-SF. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPGMB_LACLA
    AccessioniPrimary (citable) accession number: P71447
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: April 27, 2001
    Last modified: November 2, 2016
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.