PGMB_LACLA
ID PGMB_LACLA Reviewed; 221 AA.
AC P71447;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Beta-phosphoglucomutase {ECO:0000303|PubMed:9084169};
DE Short=Beta-PGM {ECO:0000303|PubMed:9084169};
DE EC=5.4.2.6 {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:9084169};
GN Name=pgmB {ECO:0000303|PubMed:9084169}; OrderedLocusNames=LL0429;
GN ORFNames=L0001;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION AS A
RP PHOSPHOGLUCOMUTASE AND IN THE CARBOHYDRATE METABOLISM, CATALYTIC ACTIVITY,
RP INDUCTION, SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RC STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
RX PubMed=9084169; DOI=10.1099/00221287-143-3-855;
RA Qian N., Stanley G.A., Bunte A., Raadstroem P.;
RT "Product formation and phosphoglucomutase activities in Lactococcus lactis:
RT cloning and characterization of a novel phosphoglucomutase gene.";
RL Microbiology 143:855-865(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [3]
RP INDUCTION, SUBSTRATE SPECIFICITY, COFACTOR, AND SUBUNIT.
RX PubMed=8071206; DOI=10.1128/jb.176.17.5304-5311.1994;
RA Qian N., Stanley G.A., Hahn-Hagerdal B., Radstrom P.;
RT "Purification and characterization of two phosphoglucomutases from
RT Lactococcus lactis subsp. lactis and their regulation in maltose- and
RT glucose-utilizing cells.";
RL J. Bacteriol. 176:5304-5311(1994).
RN [4]
RP FUNCTION AS A BETA-PHOSPHOGLUCOMUTASE, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP LYS-45; GLY-46; ARG-49 AND SER-52, AND INDUCTION.
RC STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
RX PubMed=15005616; DOI=10.1021/bi0356810;
RA Lahiri S.D., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.;
RT "Analysis of the substrate specificity loop of the HAD superfamily cap
RT domain.";
RL Biochemistry 43:2812-2820(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP REACTION MECHANISM, AND SUBUNIT.
RX PubMed=12081483; DOI=10.1021/bi0202373;
RA Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.;
RT "Caught in the act: the structure of phosphorylated beta-phosphoglucomutase
RT from Lactococcus lactis.";
RL Biochemistry 41:8351-8359(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RP AND MAGNESIUM IONS.
RX PubMed=12637673; DOI=10.1126/science.1082710;
RA Lahiri S.D., Zhang G., Dunaway-Mariano D., Allen K.N.;
RT "The pentacovalent phosphorus intermediate of a phosphoryl transfer
RT reaction.";
RL Science 299:2067-2071(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP CATALYTIC ACTIVITY, PHOSPHORYLATION AT ASP-8, MUTAGENESIS OF ASP-8 AND
RP ASP-170, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM.
RX PubMed=15996095; DOI=10.1021/bi050558p;
RA Zhang G., Dai J., Wang L., Dunaway-Mariano D., Tremblay L.W., Allen K.N.;
RT "Catalytic cycling in beta-phosphoglucomutase: a kinetic and structural
RT analysis.";
RL Biochemistry 44:9404-9416(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RP AND MAGNESIUM IONS, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=15826149; DOI=10.1021/ja0509073;
RA Tremblay L.W., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.;
RT "Chemical confirmation of a pentavalent phosphorane in complex with beta-
RT phosphoglucomutase.";
RL J. Am. Chem. Soc. 127:5298-5299(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP MUTAGENESIS OF ASP-10; THR-16; HIS-20 AND LYS-76, AND REACTION MECHANISM.
RX PubMed=19154134; DOI=10.1021/bi801653r;
RA Dai J., Finci L., Zhang C., Lahiri S., Zhang G., Peisach E., Allen K.N.,
RA Dunaway-Mariano D.;
RT "Analysis of the structural determinants underlying discrimination between
RT substrate and solvent in beta-phosphoglucomutase catalysis.";
RL Biochemistry 48:1984-1995(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RP AND MAGNESIUM IONS.
RA Bowler M.W., Baxter N.J., Webster C.E., Pollard S., Alizadeh T.,
RA Hounslow A.M., Cliff M.J., Bermel W., Williams N.H., Hollfelder F.,
RA Blackburn G.M., Waltho J.P.;
RT "The role of strain in enzyme catalysed phosphate transfer.";
RL Submitted (APR-2009) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS
RP AND MAGNESIUM IONS.
RX PubMed=20164409; DOI=10.1073/pnas.0910333106;
RA Baxter N.J., Bowler M.W., Alizadeh T., Cliff M.J., Hounslow A.M., Wu B.,
RA Berkowitz D.B., Williams N.H., Blackburn G.M., Waltho J.P.;
RT "Atomic details of near-transition state conformers for enzyme phosphoryl
RT transfer revealed by MgF-3 rather than by phosphoranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4555-4560(2010).
CC -!- FUNCTION: Catalyzes the interconversion of D-glucose 1-phosphate (G1P)
CC and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-
CC (bis)phosphate (beta-G16P) as an intermediate. The beta-
CC phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P.
CC Glucose or lactose are used in preference to maltose, which is only
CC utilized after glucose or lactose has been exhausted. It plays a key
CC role in the regulation of the flow of carbohydrate intermediates in
CC glycolysis and the formation of the sugar nucleotide UDP-glucose.
CC {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:9084169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:20113, ChEBI:CHEBI:57684, ChEBI:CHEBI:58247;
CC EC=5.4.2.6; Evidence={ECO:0000269|PubMed:15005616,
CC ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:9084169};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:8071206};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:15996095,
CC ECO:0000269|PubMed:8071206};
CC -!- ACTIVITY REGULATION: Competitively inhibited by alpha-D-galactose-1-
CC phosphate. {ECO:0000269|PubMed:15826149}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.6 uM for beta-glucose 1-phosphate (at pH 7 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:15996095};
CC KM=20 uM for alpha-D-glucose 1,6-bisphosphate (at pH 7 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:15996095};
CC KM=100 uM for alpha-D-fructose 1,6-bisphosphate (at pH 7 and 25
CC degrees Celsius) {ECO:0000269|PubMed:15996095};
CC KM=270 uM for magnesium (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15996095};
CC KM=800 uM for acetyl-phosphate (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15996095};
CC pH dependence:
CC Optimum pH is around 7. Relatively stable in solution within the pH
CC range of 5-9.5. {ECO:0000269|PubMed:15996095};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12081483,
CC ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149,
CC ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:19154134,
CC ECO:0000269|PubMed:20164409, ECO:0000269|PubMed:8071206,
CC ECO:0000269|Ref.10}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By maltose, trehalose and sucrose and repressed by glucose
CC and lactose. {ECO:0000269|PubMed:15005616, ECO:0000269|PubMed:8071206,
CC ECO:0000269|PubMed:9084169}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15996095}.
CC -!- MISCELLANEOUS: The catalysis proceeds via a phosphoenzyme formed by
CC reaction of an active-site nucleophile with the cofactor glucose 1,6-
CC diphosphate (G1,6-diP). The phosphorylated mutase binds either G1P or
CC G6P and transfers the phosphoryl group to the C(6)OH or C(1)OH,
CC respectively.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; Z70730; CAA94734.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK04527.1; -; Genomic_DNA.
DR PIR; E86678; E86678.
DR RefSeq; NP_266585.1; NC_002662.1.
DR RefSeq; WP_010905331.1; NC_002662.1.
DR PDB; 1LVH; X-ray; 2.30 A; A/B=1-221.
DR PDB; 1O03; X-ray; 1.40 A; A=1-221.
DR PDB; 1O08; X-ray; 1.20 A; A=1-221.
DR PDB; 1Z4N; X-ray; 1.97 A; A/B=1-221.
DR PDB; 1Z4O; X-ray; 1.90 A; A/B=1-221.
DR PDB; 1ZOL; X-ray; 1.90 A; A=1-221.
DR PDB; 2WF5; X-ray; 1.30 A; A=1-221.
DR PDB; 2WF6; X-ray; 1.40 A; A=1-221.
DR PDB; 2WF7; X-ray; 1.05 A; A=1-221.
DR PDB; 2WF8; X-ray; 1.20 A; A=1-221.
DR PDB; 2WF9; X-ray; 1.40 A; A=1-221.
DR PDB; 2WFA; X-ray; 1.65 A; A=1-221.
DR PDB; 2WHE; X-ray; 1.55 A; A=1-221.
DR PDB; 3FM9; X-ray; 2.70 A; A=1-221.
DR PDB; 3ZI4; X-ray; 1.33 A; A=1-221.
DR PDB; 4C4R; X-ray; 1.10 A; A=1-221.
DR PDB; 4C4S; X-ray; 1.50 A; A=1-221.
DR PDB; 4C4T; X-ray; 1.50 A; A=1-221.
DR PDB; 5O6P; X-ray; 2.20 A; A=1-221.
DR PDB; 5O6R; X-ray; 1.36 A; A=1-221.
DR PDB; 5OJZ; X-ray; 1.30 A; A=1-220.
DR PDB; 5OK0; X-ray; 2.15 A; A=1-218.
DR PDB; 5OK1; X-ray; 1.86 A; A=1-218.
DR PDB; 5OK2; X-ray; 1.10 A; A=1-218.
DR PDB; 5OLW; X-ray; 2.28 A; A/B=1-221.
DR PDB; 5OLX; X-ray; 1.38 A; A=1-221.
DR PDB; 5OLY; X-ray; 2.00 A; A/G=1-221.
DR PDB; 6H8U; X-ray; 1.90 A; A=1-221.
DR PDB; 6H8V; X-ray; 1.84 A; A/B=1-221.
DR PDB; 6H8W; X-ray; 1.98 A; A=1-221.
DR PDB; 6H8X; X-ray; 1.83 A; A/B=1-221.
DR PDB; 6H8Y; X-ray; 1.89 A; A=1-221.
DR PDB; 6H8Z; X-ray; 1.60 A; A=1-221.
DR PDB; 6H90; X-ray; 1.31 A; A=1-221.
DR PDB; 6H91; X-ray; 2.38 A; A/B=1-221.
DR PDB; 6H92; X-ray; 2.60 A; A/B=1-221.
DR PDB; 6H93; X-ray; 1.77 A; A/B=1-221.
DR PDB; 6H94; X-ray; 1.49 A; A=1-221.
DR PDB; 6HDF; X-ray; 1.40 A; A/B=1-221.
DR PDB; 6HDG; X-ray; 1.15 A; A=1-221.
DR PDB; 6HDH; X-ray; 1.62 A; A/B=1-221.
DR PDB; 6HDI; X-ray; 2.03 A; A/B=1-221.
DR PDB; 6HDJ; X-ray; 1.16 A; A=1-221.
DR PDB; 6HDK; X-ray; 1.24 A; A=1-221.
DR PDB; 6HDL; X-ray; 1.16 A; A=1-221.
DR PDB; 6HDM; X-ray; 1.30 A; A=1-221.
DR PDB; 6I03; X-ray; 1.02 A; A=1-221.
DR PDB; 6QZG; X-ray; 2.47 A; A/B=1-221.
DR PDB; 6YDJ; X-ray; 1.04 A; A=1-221.
DR PDB; 6YDK; X-ray; 2.02 A; A=1-221.
DR PDB; 6YDL; X-ray; 1.52 A; A=1-221.
DR PDB; 6YDM; X-ray; 2.10 A; A/B=1-221.
DR PDBsum; 1LVH; -.
DR PDBsum; 1O03; -.
DR PDBsum; 1O08; -.
DR PDBsum; 1Z4N; -.
DR PDBsum; 1Z4O; -.
DR PDBsum; 1ZOL; -.
DR PDBsum; 2WF5; -.
DR PDBsum; 2WF6; -.
DR PDBsum; 2WF7; -.
DR PDBsum; 2WF8; -.
DR PDBsum; 2WF9; -.
DR PDBsum; 2WFA; -.
DR PDBsum; 2WHE; -.
DR PDBsum; 3FM9; -.
DR PDBsum; 3ZI4; -.
DR PDBsum; 4C4R; -.
DR PDBsum; 4C4S; -.
DR PDBsum; 4C4T; -.
DR PDBsum; 5O6P; -.
DR PDBsum; 5O6R; -.
DR PDBsum; 5OJZ; -.
DR PDBsum; 5OK0; -.
DR PDBsum; 5OK1; -.
DR PDBsum; 5OK2; -.
DR PDBsum; 5OLW; -.
DR PDBsum; 5OLX; -.
DR PDBsum; 5OLY; -.
DR PDBsum; 6H8U; -.
DR PDBsum; 6H8V; -.
DR PDBsum; 6H8W; -.
DR PDBsum; 6H8X; -.
DR PDBsum; 6H8Y; -.
DR PDBsum; 6H8Z; -.
DR PDBsum; 6H90; -.
DR PDBsum; 6H91; -.
DR PDBsum; 6H92; -.
DR PDBsum; 6H93; -.
DR PDBsum; 6H94; -.
DR PDBsum; 6HDF; -.
DR PDBsum; 6HDG; -.
DR PDBsum; 6HDH; -.
DR PDBsum; 6HDI; -.
DR PDBsum; 6HDJ; -.
DR PDBsum; 6HDK; -.
DR PDBsum; 6HDL; -.
DR PDBsum; 6HDM; -.
DR PDBsum; 6I03; -.
DR PDBsum; 6QZG; -.
DR PDBsum; 6YDJ; -.
DR PDBsum; 6YDK; -.
DR PDBsum; 6YDL; -.
DR PDBsum; 6YDM; -.
DR AlphaFoldDB; P71447; -.
DR BMRB; P71447; -.
DR SMR; P71447; -.
DR STRING; 272623.L0001; -.
DR DrugBank; DB02317; Alpha-D-Galactose-1-Phosphate.
DR DrugBank; DB02835; Alpha-D-Glucose 1,6-Bisphosphate.
DR DrugBank; DB01857; Phosphoaspartate.
DR PaxDb; P71447; -.
DR EnsemblBacteria; AAK04527; AAK04527; L0001.
DR KEGG; lla:L0001; -.
DR PATRIC; fig|272623.7.peg.467; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_13_3_9; -.
DR OMA; TQTAKVH; -.
DR BioCyc; MetaCyc:MON-5821; -.
DR BRENDA; 5.4.2.6; 2903.
DR SABIO-RK; P71447; -.
DR EvolutionaryTrace; P71447; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR CDD; cd02598; HAD_BPGM; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR InterPro; IPR010972; Beta-phosphoglucomutase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01990; bPGM; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..221
FT /note="Beta-phosphoglucomutase"
FT /id="PRO_0000108053"
FT ACT_SITE 8
FT /note="Nucleophile"
FT ACT_SITE 10
FT /note="Proton donor"
FT BINDING 8..10
FT /ligand="substrate"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 24
FT /ligand="substrate"
FT BINDING 44..49
FT /ligand="substrate"
FT BINDING 52
FT /ligand="substrate"
FT BINDING 76
FT /ligand="substrate"
FT BINDING 114..118
FT /ligand="substrate"
FT BINDING 145
FT /ligand="substrate"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT SITE 114
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT SITE 145
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT MOD_RES 8
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000269|PubMed:15996095"
FT MUTAGEN 8
FT /note="D->A: Inactive."
FT /evidence="ECO:0000269|PubMed:15996095"
FT MUTAGEN 8
FT /note="D->E: Inactive."
FT /evidence="ECO:0000269|PubMed:15996095"
FT MUTAGEN 10
FT /note="D->A: Inactive."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 10
FT /note="D->E: Inactive."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 10
FT /note="D->N: Inactive."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 10
FT /note="D->S: Inactive."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 16
FT /note="T->P: 500-fold reduction in the rate constant for
FT Asp-8 phosphorylation by beta-G1,6bisP. 6,700-fold
FT reduction in the apparent rate constant for cycling of the
FT phosphorylated enzyme to convert beta-G1P to G6P. 13-fold
FT increase in the estimated rate constant for phosphoryl
FT transfer from the phospho-Asp8 to water."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 20
FT /note="H->A: Impairs Asp-8 phosphorylation by beta-G1,6bisP
FT and phosphoryl transfer from the phospho-Asp8 to the
FT substrate beta-G1P."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 20
FT /note="H->N: 300-fold reduction in the conversion of beta-
FT G1P to G6P in the presence of beta-G1,6bisP."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 20
FT /note="H->Q: 8-fold reduction in the conversion of beta-G1P
FT to G6P in the presence of beta-G1,6bisP."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 45
FT /note="K->A: 20'000-fold decrease in kcat/KM."
FT /evidence="ECO:0000269|PubMed:15005616"
FT MUTAGEN 46
FT /note="G->A: 1'000'000-fold decrease in kcat/KM."
FT /evidence="ECO:0000269|PubMed:15005616"
FT MUTAGEN 46
FT /note="G->P: 100'000-fold decrease in kcat/KM."
FT /evidence="ECO:0000269|PubMed:15005616"
FT MUTAGEN 46
FT /note="G->V: 10'000-fold decrease in kcat/KM."
FT /evidence="ECO:0000269|PubMed:15005616"
FT MUTAGEN 49
FT /note="R->K: 1'000'000-fold decrease in kcat/KM."
FT /evidence="ECO:0000269|PubMed:15005616"
FT MUTAGEN 52
FT /note="S->A: Wild-type activity."
FT /evidence="ECO:0000269|PubMed:15005616"
FT MUTAGEN 76
FT /note="K->A: 100-fold reduction in the conversion of beta-
FT G1P to G6P in the presence of beta-G1,6bisP."
FT /evidence="ECO:0000269|PubMed:19154134"
FT MUTAGEN 170
FT /note="D->A: Impaired, but active with an increase in the
FT affinity for G1P."
FT /evidence="ECO:0000269|PubMed:15996095"
FT CONFLICT 125
FT /note="K -> R (in Ref. 1; CAA94734)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="Y -> H (in Ref. 1; CAA94734)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6I03"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:6I03"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6I03"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:6I03"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1O08"
FT HELIX 66..83
FT /evidence="ECO:0007829|PDB:6I03"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:6I03"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6I03"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6I03"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6I03"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6I03"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:6I03"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:6I03"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:6I03"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:5OLW"
SQ 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
