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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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei8 – 81Nucleophile
    Metal bindingi8 – 81Magnesium 1
    Metal bindingi8 – 81Magnesium 2
    Active sitei10 – 101Proton donor
    Metal bindingi10 – 101Magnesium 1
    Metal bindingi10 – 101Magnesium 2; via carbonyl oxygen
    Binding sitei24 – 241Substrate
    Binding sitei52 – 521Substrate
    Binding sitei76 – 761Substrate
    Sitei114 – 1141Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups
    Binding sitei145 – 1451Substrate
    Sitei145 – 1451Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups
    Metal bindingi169 – 1691Magnesium 1
    Metal bindingi170 – 1701Magnesium 1
    Metal bindingi170 – 1701Magnesium 2

    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

    BioCyciLLAC272623:GHSH-459-MONOMER.
    MetaCyc: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
    ProteomesiUP000002196 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81D → A: Inactive. 1 Publication
    Mutagenesisi8 – 81D → E: Inactive. 1 Publication
    Mutagenesisi10 – 101D → A: Inactive. 1 Publication
    Mutagenesisi10 – 101D → E: Inactive. 1 Publication
    Mutagenesisi10 – 101D → N: Inactive. 1 Publication
    Mutagenesisi10 – 101D → S: Inactive. 1 Publication
    Mutagenesisi16 – 161T → 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 Publication
    Mutagenesisi20 – 201H → A: Impairs Asp-8 phosphorylation by beta-G1,6bisP and phosphoryl transfer from the phospho-Asp8 to the substrate beta-G1P. 1 Publication
    Mutagenesisi20 – 201H → N: 300-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. 1 Publication
    Mutagenesisi20 – 201H → Q: 8-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. 1 Publication
    Mutagenesisi45 – 451K → A: 20'000-fold decrease in Kcat/KM. 1 Publication
    Mutagenesisi46 – 461G → A: 1'000'000-fold decrease in Kcat/KM. 1 Publication
    Mutagenesisi46 – 461G → P: 100'000-fold decrease in Kcat/KM. 1 Publication
    Mutagenesisi46 – 461G → V: 10'000-fold decrease in Kcat/KM. 1 Publication
    Mutagenesisi49 – 491R → K: 1'000'000-fold decrease in Kcat/KM. 1 Publication
    Mutagenesisi52 – 521S → A: Wild-type activity. 1 Publication
    Mutagenesisi76 – 761K → A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. 1 Publication
    Mutagenesisi170 – 1701D → A: Impaired, but active with an increase in the affinity for G1P. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 221221Beta-phosphoglucomutasePRO_0000108053Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 814-aspartylphosphate1 Publication

    Post-translational modificationi

    Autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    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

    1
    221
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74Combined sources
    Turni10 – 123Combined sources
    Beta strandi13 – 153Combined sources
    Helixi16 – 3015Combined sources
    Helixi38 – 414Combined sources
    Turni42 – 465Combined sources
    Helixi49 – 5911Combined sources
    Beta strandi60 – 623Combined sources
    Helixi66 – 8318Combined sources
    Helixi84 – 863Combined sources
    Helixi89 – 913Combined sources
    Helixi96 – 10510Combined sources
    Beta strandi109 – 1124Combined sources
    Helixi119 – 1257Combined sources
    Helixi129 – 1313Combined sources
    Beta strandi133 – 1353Combined sources
    Turni138 – 1403Combined sources
    Beta strandi141 – 1433Combined sources
    Helixi149 – 1579Combined sources
    Helixi162 – 1643Combined sources
    Beta strandi165 – 1717Combined sources
    Helixi172 – 18110Combined sources
    Beta strandi184 – 1896Combined sources
    Helixi191 – 1944Combined sources
    Beta strandi196 – 2038Combined sources
    Helixi204 – 2063Combined sources
    Helixi209 – 2179Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP71447.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni8 – 103Substrate binding
    Regioni44 – 496Substrate binding
    Regioni114 – 1185Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0637.
    KOiK01838.
    OMAiLHRGKPD.
    OrthoDBiEOG6KMBB8.

    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]
    PfamiPF00702. Hydrolase. 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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti125 – 1251K → R in CAA94734 (PubMed:9084169).Curated
    Sequence conflicti206 – 2061Y → H in CAA94734 (PubMed:9084169).Curated

    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
    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. Positions 1-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272623.L0001.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiCOG0637.
    KOiK01838.
    OMAiLHRGKPD.
    OrthoDBiEOG6KMBB8.

    Enzyme and pathway databases

    BioCyciLLAC272623:GHSH-459-MONOMER.
    MetaCyc:MONOMER-5821.
    BRENDAi5.4.2.6. 2903.
    SABIO-RKP71447.

    Miscellaneous databases

    EvolutionaryTraceiP71447.
    PROiP71447.

    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]
    PfamiPF00702. Hydrolase. 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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Product formation and phosphoglucomutase activities in Lactococcus lactis: cloning and characterization of a novel phosphoglucomutase gene."
      Qian N., Stanley G.A., Bunte A., Raadstroem P.
      Microbiology 143:855-865(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION AS A PHOSPHOGLUCOMUTASE AND IN THE CARBOHYDRATE METABOLISM, INDUCTION, SUBSTRATE SPECIFICITY, NOMENCLATURE.
      Strain: ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681.
    2. "The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
      Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
      Genome Res. 11:731-753(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: IL1403.
    3. "Purification and characterization of two phosphoglucomutases from Lactococcus lactis subsp. lactis and their regulation in maltose- and glucose-utilizing cells."
      Qian N., Stanley G.A., Hahn-Hagerdal B., Radstrom P.
      J. Bacteriol. 176:5304-5311(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT.
    4. "Analysis of the substrate specificity loop of the HAD superfamily cap domain."
      Lahiri S.D., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.
      Biochemistry 43:2812-2820(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A BETA-PHOSPHOGLUCOMUTASE, MUTAGENESIS OF LYS-45; GLY-46; ARG-49 AND SER-52, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681.
    5. "Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis."
      Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.
      Biochemistry 41:8351-8359(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, REACTION MECHANISM, SUBUNIT.
    6. "The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction."
      Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.
      Science 299:2067-2071(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS.
    7. "Catalytic cycling in beta-phosphoglucomutase: a kinetic and structural analysis."
      Zhang G., Dai J., Wang L., Dunaway-Mariano D., Tremblay L.W., Allen K.N.
      Biochemistry 44:9404-9416(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, PHOSPHORYLATION AT ASP-8, MUTAGENESIS OF ASP-8 AND ASP-170, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
    8. "Chemical confirmation of a pentavalent phosphorane in complex with beta-phosphoglucomutase."
      Tremblay L.W., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.
      J. Am. Chem. Soc. 127:5298-5299(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS, ENZYME REGULATION, SUBUNIT.
    9. "Analysis of the structural determinants underlying discrimination between substrate and solvent in beta-phosphoglucomutase catalysis."
      Dai J., Finci L., Zhang C., Lahiri S., Zhang G., Peisach E., Allen K.N., Dunaway-Mariano D.
      Biochemistry 48:1984-1995(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, MUTAGENESIS OF ASP-10; THR-16; HIS-20 AND LYS-76, REACTION MECHANISM.
    10. "The role of strain in enzyme catalysed phosphate transfer."
      Bowler M.W., Baxter N.J., Webster C.E., Pollard S., Alizadeh T., Hounslow A.M., Cliff M.J., Bermel W., Williams N.H., Hollfelder F., Blackburn G.M., Waltho J.P.
      Submitted (APR-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS.
    11. "Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF-3 rather than by phosphoranes."
      Baxter N.J., Bowler M.W., Alizadeh T., Cliff M.J., Hounslow A.M., Wu B., Berkowitz D.B., Williams N.H., Blackburn G.M., Waltho J.P.
      Proc. Natl. Acad. Sci. U.S.A. 107:4555-4560(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS.

    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: April 29, 2015
    This is version 115 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

    External Data

    Dasty 3

    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 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.