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P71447

- PGMB_LACLA

UniProt

P71447 - PGMB_LACLA

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Protein

Beta-phosphoglucomutase

Gene
pgmB, LL0429, L0001
Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Status
Reviewed - 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

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

pH dependencei

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

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

  1. beta-phosphoglucomutase activity Source: UniProtKB
  2. hydrolase activity Source: InterPro
  3. magnesium ion binding Source: UniProtKB

GO - Biological processi

  1. 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: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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-aspartylphosphate

Post-translational modificationi

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Expressioni

Inductioni

By maltose, trehalose and sucrose and repressed by glucose and lactose.4 Publications

Interactioni

Subunit structurei

Monomer.3 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 – 74
Turni10 – 123
Beta strandi13 – 153
Helixi16 – 3015
Helixi38 – 414
Turni42 – 465
Helixi49 – 5911
Beta strandi60 – 623
Helixi66 – 8318
Helixi84 – 863
Helixi89 – 913
Helixi96 – 10510
Beta strandi109 – 1124
Helixi119 – 1257
Helixi129 – 1313
Beta strandi133 – 1353
Turni138 – 1403
Beta strandi141 – 1433
Helixi149 – 1579
Helixi162 – 1643
Beta strandi165 – 1717
Helixi172 – 18110
Beta strandi184 – 1896
Helixi191 – 1944
Beta strandi196 – 2038
Helixi204 – 2063
Helixi209 – 2179

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP71447.
SMRiP71447. Positions 1-221.

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.
OMAiAGGHEND.
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

MFKAVLFDLD GVITDTAEYH FRAWKALAEE IGINGVDRQF NEQLKGVSRE    50
DSLQKILDLA DKKVSAEEFK ELAKRKNDNY VKMIQDVSPA DVYPGILQLL 100
KDLRSNKIKI ALASASKNGP FLLEKMNLTG YFDAIADPAE VAASKPAPDI 150
FIAAAHAVGV APSESIGLED SQAGIQAIKD SGALPIGVGR PEDLGDDIVI 200
VPDTSYYTLE FLKEVWLQKQ K 221
Length:221
Mass (Da):24,209
Last modified:April 27, 2001 - v2
Checksum:i53AC0BF0FA249EFC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251K → R in CAA94734. 1 Publication
Sequence conflicti206 – 2061Y → H in CAA94734. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z70730 Genomic DNA. Translation: CAA94734.1.
AE005176 Genomic DNA. Translation: AAK04527.1.
PIRiE86678.
RefSeqiNP_266585.1. NC_002662.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z70730 Genomic DNA. Translation: CAA94734.1 .
AE005176 Genomic DNA. Translation: AAK04527.1 .
PIRi E86678.
RefSeqi NP_266585.1. NC_002662.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LVH X-ray 2.30 A/B 1-221 [» ]
1O03 X-ray 1.40 A 1-221 [» ]
1O08 X-ray 1.20 A 1-221 [» ]
1Z4N X-ray 1.97 A/B 1-221 [» ]
1Z4O X-ray 1.90 A/B 1-221 [» ]
1ZOL X-ray 1.90 A 1-221 [» ]
2WF5 X-ray 1.30 A 1-221 [» ]
2WF6 X-ray 1.40 A 1-221 [» ]
2WF7 X-ray 1.05 A 1-221 [» ]
2WF8 X-ray 1.20 A 1-221 [» ]
2WF9 X-ray 1.40 A 1-221 [» ]
2WFA X-ray 1.65 A 1-221 [» ]
2WHE X-ray 1.55 A 1-221 [» ]
3FM9 X-ray 2.70 A 1-221 [» ]
3ZI4 X-ray 1.33 A 1-221 [» ]
ProteinModelPortali P71447.
SMRi P71447. Positions 1-221.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272623.L0001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK04527 ; AAK04527 ; L0001 .
GeneIDi 1114041.
KEGGi lla:L0001.
PATRICi 22293074. VBILacLac136773_0467.

Phylogenomic databases

eggNOGi COG0637.
KOi K01838.
OMAi AGGHEND.
OrthoDBi EOG6KMBB8.

Enzyme and pathway databases

BioCyci LLAC272623:GHSH-459-MONOMER.
MetaCyc:MONOMER-5821.
BRENDAi 5.4.2.6. 2903.
SABIO-RK P71447.

Miscellaneous databases

EvolutionaryTracei P71447.
PROi P71447.

Family and domain databases

Gene3Di 1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
InterProi IPR010976. B-phosphoglucomutase_hydrolase.
IPR010972. Beta-phosphoglucomutase.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
[Graphical view ]
Pfami PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00413. HADHALOGNASE.
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01990. bPGM. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR02009. PGMB-YQAB-SF. 1 hit.
ProtoNeti Search...

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 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.

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: May 14, 2014
This is version 108 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

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