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P71447 (PGMB_LACLA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-phosphoglucomutase

Short name=Beta-PGM
EC=5.4.2.6
Gene names
Name:pgmB
Ordered Locus Names:LL0429
ORF Names:L0001
OrganismLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) [Reference proteome] [HAMAP]
Taxonomic identifier272623 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per subunit. Ref.3 Ref.7

Enzyme regulation

Competitively inhibited by alpha-D-galactose-1-phosphate. Ref.8

Subunit structure

Monomer. Ref.3 Ref.5 Ref.8

Subcellular location

Cytoplasm Potential.

Induction

By maltose, trehalose and sucrose and repressed by glucose and lactose. Ref.1 Ref.3 Ref.4 Ref.8

Post-translational modification

Autophosphorylated.

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.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.

Biophysicochemical properties

Kinetic parameters:

KM=14.6 µM for beta-glucose 1-phosphate (at pH 7 and 25 degrees Celsius) Ref.4 Ref.7

KM=20 µM for alpha-D-glucose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius)

KM=100 µM for alpha-D-fructose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius)

KM=270 µM for magnesium (at pH 7 and 25 degrees Celsius)

KM=800 µM for acetyl-phosphate (at pH 7 and 25 degrees Celsius)

pH dependence:

Optimum pH is around 7. Relatively stable in solution within the pH range of 5-9.5.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-phosphoglucomutase activity

Inferred from direct assay Ref.4. Source: UniProtKB

hydrolase activity

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Beta-phosphoglucomutase
PRO_0000108053

Regions

Region8 – 103Substrate binding
Region44 – 496Substrate binding
Region114 – 1185Substrate binding

Sites

Active site81Nucleophile
Active site101Proton donor
Metal binding81Magnesium 1
Metal binding81Magnesium 2
Metal binding101Magnesium 1
Metal binding101Magnesium 2; via carbonyl oxygen
Metal binding1691Magnesium 1
Metal binding1701Magnesium 1
Metal binding1701Magnesium 2
Binding site241Substrate
Binding site521Substrate
Binding site761Substrate
Binding site1451Substrate
Site1141Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups
Site1451Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups

Amino acid modifications

Modified residue814-aspartylphosphate

Experimental info

Mutagenesis81D → A: Inactive. Ref.7
Mutagenesis81D → E: Inactive. Ref.7
Mutagenesis101D → A: Inactive. Ref.9
Mutagenesis101D → E: Inactive. Ref.9
Mutagenesis101D → N: Inactive. Ref.9
Mutagenesis101D → S: Inactive. Ref.9
Mutagenesis161T → 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. Ref.9
Mutagenesis201H → A: Impairs Asp-8 phosphorylation by beta-G1,6bisP and phosphoryl transfer from the phospho-Asp8 to the substrate beta-G1P. Ref.9
Mutagenesis201H → N: 300-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. Ref.9
Mutagenesis201H → Q: 8-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. Ref.9
Mutagenesis451K → A: 20'000-fold decrease in Kcat/KM. Ref.4
Mutagenesis461G → A: 1'000'000-fold decrease in Kcat/KM. Ref.4
Mutagenesis461G → P: 100'000-fold decrease in Kcat/KM. Ref.4
Mutagenesis461G → V: 10'000-fold decrease in Kcat/KM. Ref.4
Mutagenesis491R → K: 1'000'000-fold decrease in Kcat/KM. Ref.4
Mutagenesis521S → A: Wild-type activity. Ref.4
Mutagenesis761K → A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP. Ref.9
Mutagenesis1701D → A: Impaired, but active with an increase in the affinity for G1P. Ref.7
Sequence conflict1251K → R in CAA94734. Ref.1
Sequence conflict2061Y → H in CAA94734. Ref.1

Secondary structure

.............................................. 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P71447 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 53AC0BF0FA249EFC

FASTA22124,209
        10         20         30         40         50         60 
MFKAVLFDLD GVITDTAEYH FRAWKALAEE IGINGVDRQF NEQLKGVSRE DSLQKILDLA 

        70         80         90        100        110        120 
DKKVSAEEFK ELAKRKNDNY VKMIQDVSPA DVYPGILQLL KDLRSNKIKI ALASASKNGP 

       130        140        150        160        170        180 
FLLEKMNLTG YFDAIADPAE VAASKPAPDI FIAAAHAVGV APSESIGLED SQAGIQAIKD 

       190        200        210        220 
SGALPIGVGR PEDLGDDIVI VPDTSYYTLE FLKEVWLQKQ K 

« Hide

References

« Hide 'large scale' references
[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 MECAHNISM, 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, 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z70730 Genomic DNA. Translation: CAA94734.1.
AE005176 Genomic DNA. Translation: AAK04527.1.
PIRE86678.
RefSeqNP_266585.1. NC_002662.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP71447.
SMRP71447. Positions 1-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272623.L0001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK04527; AAK04527; L0001.
GeneID1114041.
KEGGlla:L0001.
PATRIC22293074. VBILacLac136773_0467.

Phylogenomic databases

eggNOGCOG0637.
KOK01838.
OMAEEIGING.
OrthoDBEOG6KMBB8.
ProtClustDBCLSK876745.

Enzyme and pathway databases

BioCycLLAC272623:GHSH-459-MONOMER.
MetaCyc:MONOMER-5821.
BRENDA5.4.2.6. 2903.
SABIO-RKP71447.

Family and domain databases

Gene3D1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR010976. B-phosphoglucomutase_hydrolase.
IPR010972. Beta-phosphoglucomutase.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
[Graphical view]
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00413. HADHALOGNASE.
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01990. bPGM. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR02009. PGMB-YQAB-SF. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP71447.
PROP71447.

Entry information

Entry namePGMB_LACLA
AccessionPrimary (citable) accession number: P71447
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 27, 2001
Last modified: March 19, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references