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Beta-phosphoglucomutase (Beta-PGM) (EC 5.4.2.6)

 PGMB_LACLA              Reviewed;         221 AA.
P71447;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
25-OCT-2017, entry version 128.
RecName: Full=Beta-phosphoglucomutase;
Short=Beta-PGM;
EC=5.4.2.6;
Name=pgmB; OrderedLocusNames=LL0429; ORFNames=L0001;
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
lactis).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Lactococcus.
NCBI_TaxID=272623;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION
AS A PHOSPHOGLUCOMUTASE AND IN THE CARBOHYDRATE METABOLISM, INDUCTION,
SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
PubMed=9084169; DOI=10.1099/00221287-143-3-855;
Qian N., Stanley G.A., Bunte A., Raadstroem P.;
"Product formation and phosphoglucomutase activities in Lactococcus
lactis: cloning and characterization of a novel phosphoglucomutase
gene.";
Microbiology 143:855-865(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IL1403;
PubMed=11337471; DOI=10.1101/gr.GR-1697R;
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
Weissenbach J., Ehrlich S.D., Sorokin A.;
"The complete genome sequence of the lactic acid bacterium Lactococcus
lactis ssp. lactis IL1403.";
Genome Res. 11:731-753(2001).
[3]
INDUCTION, SUBSTRATE SPECIFICITY, COFACTOR, AND SUBUNIT.
PubMed=8071206; DOI=10.1128/jb.176.17.5304-5311.1994;
Qian N., Stanley G.A., Hahn-Hagerdal B., Radstrom P.;
"Purification and characterization of two phosphoglucomutases from
Lactococcus lactis subsp. lactis and their regulation in maltose- and
glucose-utilizing cells.";
J. Bacteriol. 176:5304-5311(1994).
[4]
FUNCTION AS A BETA-PHOSPHOGLUCOMUTASE, MUTAGENESIS OF LYS-45; GLY-46;
ARG-49 AND SER-52, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
PubMed=15005616; DOI=10.1021/bi0356810;
Lahiri S.D., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.;
"Analysis of the substrate specificity loop of the HAD superfamily cap
domain.";
Biochemistry 43:2812-2820(2004).
[5]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
REACTION MECHANISM, AND SUBUNIT.
PubMed=12081483; DOI=10.1021/bi0202373;
Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.;
"Caught in the act: the structure of phosphorylated beta-
phosphoglucomutase from Lactococcus lactis.";
Biochemistry 41:8351-8359(2002).
[6]
X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS AND MAGNESIUM IONS.
PubMed=12637673; DOI=10.1126/science.1082710;
Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.;
"The pentacovalent phosphorus intermediate of a phosphoryl transfer
reaction.";
Science 299:2067-2071(2003).
[7]
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, AND REACTION MECHANISM.
PubMed=15996095; DOI=10.1021/bi050558p;
Zhang G., Dai J., Wang L., Dunaway-Mariano D., Tremblay L.W.,
Allen K.N.;
"Catalytic cycling in beta-phosphoglucomutase: a kinetic and
structural analysis.";
Biochemistry 44:9404-9416(2005).
[8]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS AND MAGNESIUM IONS, ENZYME REGULATION, AND SUBUNIT.
PubMed=15826149; DOI=10.1021/ja0509073;
Tremblay L.W., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.;
"Chemical confirmation of a pentavalent phosphorane in complex with
beta-phosphoglucomutase.";
J. Am. Chem. Soc. 127:5298-5299(2005).
[9]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
MUTAGENESIS OF ASP-10; THR-16; HIS-20 AND LYS-76, AND REACTION
MECHANISM.
PubMed=19154134; DOI=10.1021/bi801653r;
Dai J., Finci L., Zhang C., Lahiri S., Zhang G., Peisach E.,
Allen K.N., Dunaway-Mariano D.;
"Analysis of the structural determinants underlying discrimination
between substrate and solvent in beta-phosphoglucomutase catalysis.";
Biochemistry 48:1984-1995(2009).
[10]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS AND MAGNESIUM IONS.
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.;
"The role of strain in enzyme catalysed phosphate transfer.";
Submitted (APR-2009) to the PDB data bank.
[11]
X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS AND MAGNESIUM IONS.
PubMed=20164409; DOI=10.1073/pnas.0910333106;
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.;
"Atomic details of near-transition state conformers for enzyme
phosphoryl transfer revealed by MgF-3 rather than by phosphoranes.";
Proc. Natl. Acad. Sci. U.S.A. 107:4555-4560(2010).
-!- 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-C(1) 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. {ECO:0000269|PubMed:15005616,
ECO:0000269|PubMed:9084169}.
-!- CATALYTIC ACTIVITY: Beta-D-glucose 1-phosphate = beta-D-glucose 6-
phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15996095,
ECO:0000269|PubMed:8071206};
Note=Binds 2 magnesium ions per subunit.
{ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:8071206};
-!- ENZYME REGULATION: Competitively inhibited by alpha-D-galactose-1-
phosphate. {ECO:0000269|PubMed:15826149}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14.6 uM for beta-glucose 1-phosphate (at pH 7 and 25 degrees
Celsius) {ECO:0000269|PubMed:15005616,
ECO:0000269|PubMed:15996095};
KM=20 uM for alpha-D-glucose 1,6-bisphosphate (at pH 7 and 25
degrees Celsius) {ECO:0000269|PubMed:15005616,
ECO:0000269|PubMed:15996095};
KM=100 uM for alpha-D-fructose 1,6-bisphosphate (at pH 7 and 25
degrees Celsius) {ECO:0000269|PubMed:15005616,
ECO:0000269|PubMed:15996095};
KM=270 uM for magnesium (at pH 7 and 25 degrees Celsius)
{ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095};
KM=800 uM for acetyl-phosphate (at pH 7 and 25 degrees Celsius)
{ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095};
pH dependence:
Optimum pH is around 7. Relatively stable in solution within the
pH range of 5-9.5. {ECO:0000269|PubMed:15005616,
ECO:0000269|PubMed:15996095};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12081483,
ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149,
ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:19154134,
ECO:0000269|PubMed:20164409, ECO:0000269|PubMed:8071206,
ECO:0000269|Ref.10}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- INDUCTION: By maltose, trehalose and sucrose and repressed by
glucose and lactose. {ECO:0000269|PubMed:15005616,
ECO:0000269|PubMed:8071206, ECO:0000269|PubMed:9084169}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15996095}.
-!- 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
C(6)OH or C(1)OH, respectively.
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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EMBL; Z70730; CAA94734.1; -; Genomic_DNA.
EMBL; AE005176; AAK04527.1; -; Genomic_DNA.
PIR; E86678; E86678.
RefSeq; NP_266585.1; NC_002662.1.
RefSeq; WP_010905331.1; NC_002662.1.
PDB; 1LVH; X-ray; 2.30 A; A/B=1-221.
PDB; 1O03; X-ray; 1.40 A; A=1-221.
PDB; 1O08; X-ray; 1.20 A; A=1-221.
PDB; 1Z4N; X-ray; 1.97 A; A/B=1-221.
PDB; 1Z4O; X-ray; 1.90 A; A/B=1-221.
PDB; 1ZOL; X-ray; 1.90 A; A=1-221.
PDB; 2WF5; X-ray; 1.30 A; A=1-221.
PDB; 2WF6; X-ray; 1.40 A; A=1-221.
PDB; 2WF7; X-ray; 1.05 A; A=1-221.
PDB; 2WF8; X-ray; 1.20 A; A=1-221.
PDB; 2WF9; X-ray; 1.40 A; A=1-221.
PDB; 2WFA; X-ray; 1.65 A; A=1-221.
PDB; 2WHE; X-ray; 1.55 A; A=1-221.
PDB; 3FM9; X-ray; 2.70 A; A=1-221.
PDB; 3ZI4; X-ray; 1.33 A; A=1-221.
PDB; 4C4R; X-ray; 1.10 A; A=1-221.
PDB; 4C4S; X-ray; 1.50 A; A=1-221.
PDB; 4C4T; X-ray; 1.50 A; A=1-221.
PDBsum; 1LVH; -.
PDBsum; 1O03; -.
PDBsum; 1O08; -.
PDBsum; 1Z4N; -.
PDBsum; 1Z4O; -.
PDBsum; 1ZOL; -.
PDBsum; 2WF5; -.
PDBsum; 2WF6; -.
PDBsum; 2WF7; -.
PDBsum; 2WF8; -.
PDBsum; 2WF9; -.
PDBsum; 2WFA; -.
PDBsum; 2WHE; -.
PDBsum; 3FM9; -.
PDBsum; 3ZI4; -.
PDBsum; 4C4R; -.
PDBsum; 4C4S; -.
PDBsum; 4C4T; -.
ProteinModelPortal; P71447; -.
SMR; P71447; -.
STRING; 272623.L0001; -.
DrugBank; DB02317; Alpha-D-Galactose-1-Phosphate.
DrugBank; DB01857; Phosphoaspartate.
PaxDb; P71447; -.
EnsemblBacteria; AAK04527; AAK04527; L0001.
GeneID; 1114041; -.
KEGG; lla:L0001; -.
PATRIC; fig|272623.7.peg.467; -.
eggNOG; ENOG4107URF; Bacteria.
eggNOG; COG0637; LUCA.
KO; K01838; -.
OMA; DTEPLHA; -.
BioCyc; MetaCyc:MONOMER-5821; -.
BRENDA; 5.4.2.6; 2903.
SABIO-RK; P71447; -.
EvolutionaryTrace; P71447; -.
Proteomes; UP000002196; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008801; F:beta-phosphoglucomutase activity; IDA:UniProtKB.
GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
Gene3D; 1.10.150.240; -; 1.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
InterPro; IPR010972; Beta-phosphoglucomutase.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006439; HAD-SF_hydro_IA.
InterPro; IPR023214; HAD_sf.
InterPro; IPR023198; PGP_dom2.
PRINTS; PR00413; HADHALOGNASE.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01990; bPGM; 1.
TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm;
Direct protein sequencing; Isomerase; Magnesium; Metal-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 221 Beta-phosphoglucomutase.
/FTId=PRO_0000108053.
REGION 8 10 Substrate binding.
REGION 44 49 Substrate binding.
REGION 114 118 Substrate binding.
ACT_SITE 8 8 Nucleophile.
ACT_SITE 10 10 Proton donor.
METAL 8 8 Magnesium 1.
METAL 8 8 Magnesium 2.
METAL 10 10 Magnesium 1.
METAL 10 10 Magnesium 2; via carbonyl oxygen.
METAL 169 169 Magnesium 1.
METAL 170 170 Magnesium 1.
METAL 170 170 Magnesium 2.
BINDING 24 24 Substrate.
BINDING 52 52 Substrate.
BINDING 76 76 Substrate.
BINDING 145 145 Substrate.
SITE 114 114 Important for catalytic activity and
assists the phosphoryl transfer reaction
to Asp8 by balancing charge and orienting
the reacting groups.
SITE 145 145 Important for catalytic activity and
assists the phosphoryl transfer reaction
to Asp8 by balancing charge and orienting
the reacting groups.
MOD_RES 8 8 4-aspartylphosphate.
{ECO:0000269|PubMed:15996095}.
MUTAGEN 8 8 D->A: Inactive.
{ECO:0000269|PubMed:15996095}.
MUTAGEN 8 8 D->E: Inactive.
{ECO:0000269|PubMed:15996095}.
MUTAGEN 10 10 D->A: Inactive.
{ECO:0000269|PubMed:19154134}.
MUTAGEN 10 10 D->E: Inactive.
{ECO:0000269|PubMed:19154134}.
MUTAGEN 10 10 D->N: Inactive.
{ECO:0000269|PubMed:19154134}.
MUTAGEN 10 10 D->S: Inactive.
{ECO:0000269|PubMed:19154134}.
MUTAGEN 16 16 T->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.
{ECO:0000269|PubMed:19154134}.
MUTAGEN 20 20 H->A: Impairs Asp-8 phosphorylation by
beta-G1,6bisP and phosphoryl transfer
from the phospho-Asp8 to the substrate
beta-G1P. {ECO:0000269|PubMed:19154134}.
MUTAGEN 20 20 H->N: 300-fold reduction in the
conversion of beta-G1P to G6P in the
presence of beta-G1,6bisP.
{ECO:0000269|PubMed:19154134}.
MUTAGEN 20 20 H->Q: 8-fold reduction in the conversion
of beta-G1P to G6P in the presence of
beta-G1,6bisP.
{ECO:0000269|PubMed:19154134}.
MUTAGEN 45 45 K->A: 20'000-fold decrease in Kcat/KM.
{ECO:0000269|PubMed:15005616}.
MUTAGEN 46 46 G->A: 1'000'000-fold decrease in Kcat/KM.
{ECO:0000269|PubMed:15005616}.
MUTAGEN 46 46 G->P: 100'000-fold decrease in Kcat/KM.
{ECO:0000269|PubMed:15005616}.
MUTAGEN 46 46 G->V: 10'000-fold decrease in Kcat/KM.
{ECO:0000269|PubMed:15005616}.
MUTAGEN 49 49 R->K: 1'000'000-fold decrease in Kcat/KM.
{ECO:0000269|PubMed:15005616}.
MUTAGEN 52 52 S->A: Wild-type activity.
{ECO:0000269|PubMed:15005616}.
MUTAGEN 76 76 K->A: 100-fold reduction in the
conversion of beta-G1P to G6P in the
presence of beta-G1,6bisP.
{ECO:0000269|PubMed:19154134}.
MUTAGEN 170 170 D->A: Impaired, but active with an
increase in the affinity for G1P.
{ECO:0000269|PubMed:15996095}.
CONFLICT 125 125 K -> R (in Ref. 1; CAA94734).
{ECO:0000305}.
CONFLICT 206 206 Y -> H (in Ref. 1; CAA94734).
{ECO:0000305}.
STRAND 4 7 {ECO:0000244|PDB:2WF7}.
TURN 10 12 {ECO:0000244|PDB:2WF7}.
STRAND 13 15 {ECO:0000244|PDB:2WF7}.
HELIX 16 30 {ECO:0000244|PDB:2WF7}.
HELIX 38 41 {ECO:0000244|PDB:2WF7}.
TURN 42 46 {ECO:0000244|PDB:2WF7}.
HELIX 49 59 {ECO:0000244|PDB:2WF7}.
STRAND 60 62 {ECO:0000244|PDB:1O08}.
HELIX 66 83 {ECO:0000244|PDB:2WF7}.
HELIX 84 86 {ECO:0000244|PDB:2WF7}.
HELIX 89 91 {ECO:0000244|PDB:2WF7}.
HELIX 96 105 {ECO:0000244|PDB:2WF7}.
STRAND 109 112 {ECO:0000244|PDB:2WF7}.
HELIX 119 125 {ECO:0000244|PDB:2WF7}.
HELIX 129 131 {ECO:0000244|PDB:2WF7}.
STRAND 133 135 {ECO:0000244|PDB:2WF7}.
TURN 138 140 {ECO:0000244|PDB:2WF7}.
STRAND 141 143 {ECO:0000244|PDB:2WF7}.
HELIX 149 157 {ECO:0000244|PDB:2WF7}.
HELIX 162 164 {ECO:0000244|PDB:2WF7}.
STRAND 165 171 {ECO:0000244|PDB:2WF7}.
HELIX 172 181 {ECO:0000244|PDB:2WF7}.
STRAND 184 189 {ECO:0000244|PDB:2WF7}.
HELIX 191 194 {ECO:0000244|PDB:2WF7}.
STRAND 196 203 {ECO:0000244|PDB:2WF7}.
HELIX 204 206 {ECO:0000244|PDB:2WF7}.
HELIX 209 217 {ECO:0000244|PDB:2WF7}.
SEQUENCE 221 AA; 24209 MW; 53AC0BF0FA249EFC CRC64;
MFKAVLFDLD GVITDTAEYH FRAWKALAEE IGINGVDRQF NEQLKGVSRE DSLQKILDLA
DKKVSAEEFK ELAKRKNDNY VKMIQDVSPA DVYPGILQLL KDLRSNKIKI ALASASKNGP
FLLEKMNLTG YFDAIADPAE VAASKPAPDI FIAAAHAVGV APSESIGLED SQAGIQAIKD
SGALPIGVGR PEDLGDDIVI VPDTSYYTLE FLKEVWLQKQ K


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