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 02-SEP-2026, entry version 166. 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; Bacillati; Bacillota; 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, INDUCTION, AND RP MUTAGENESIS OF LYS-45; GLY-46; ARG-49 AND SER-52. 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] {ECO:0007744|PDB:1LVH} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, RP REACTION MECHANISM, COFACTOR, 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] {ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08} RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS RP AND MAGNESIUM IONS, COFACTOR, AND SUBUNIT. 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] {ECO:0007744|PDB:1ZOL} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, PHOSPHORYLATION AT RP ASP-8, MUTAGENESIS OF ASP-8 AND ASP-170, BIOPHYSICOCHEMICAL PROPERTIES, RP REACTION MECHANISM, SUBUNIT, AND ACTIVE SITE. 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] {ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS RP AND MAGNESIUM IONS, ACTIVITY REGULATION, SUBUNIT, AND COFACTOR. 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] {ECO:0007744|PDB:3FM9} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, RP REACTION MECHANISM, COFACTOR, SUBUNIT, PHOSPHORYLATION AT ASP-8, ACTIVE RP SITE, AND MUTAGENESIS OF ASP-10; THR-16; HIS-20 AND LYS-76. 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] {ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6, ECO:0007744|PDB:2WHE} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH BETA-D-GLUCOSE RP 6-PHOSPHATE AND MAGNESIUM IONS, COFACTOR, AND SUBUNIT. 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:12081483, ECO:0000269|PubMed:12637673, CC ECO:0000269|PubMed:15826149, ECO:0000269|PubMed:15996095, CC ECO:0000269|PubMed:19154134, ECO:0000269|PubMed:20164409, CC ECO:0000269|PubMed:8071206}; CC Note=Binds 1 magnesium ion per subunit. {ECO:0000269|PubMed:12081483, CC ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149, CC ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:20164409}; CC -!- ACTIVITY REGULATION: Activated by phosphorylation (PubMed:15996095). CC Competitively inhibited by alpha-D-galactose-1-phosphate. CC {ECO:0000269|PubMed:15826149, ECO:0000269|PubMed:15996095}. 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 ECO:0000269|PubMed:19154134}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z70730; CAA94734.1; -; Genomic_DNA. DR EMBL; AE005176; AAK04527.1; -; Genomic_DNA. DR PIR; E86678; E86678. 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 PDB; 8Q1C; X-ray; 1.68 A; A/B=1-221. DR PDB; 8Q1D; X-ray; 1.75 A; A=1-221. DR PDB; 8Q1E; X-ray; 1.23 A; A=1-221. DR PDB; 8Q1F; X-ray; 1.01 A; A/B=1-221. DR AlphaFoldDB; P71447; -. DR BMRB; P71447; -. DR MDposit; P71447; -. DR SMR; P71447; -. DR DrugBank; DB02317; Alpha-D-Galactose-1-Phosphate. DR DrugBank; DB02835; Alpha-D-Glucose 1,6-Bisphosphate. DR DrugBank; DB01857; Phosphoaspartate. 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 OrthoDB; 9797743at2; -. DR BioCyc; MetaCyc:MONOMER-5821; -. DR BRENDA; 5.4.2.6; 2864. 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 FunFam; 1.10.150.240:FF:000010; Beta-phosphoglucomutase; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR Gene3D; 1.10.150.240; Putative phosphatase, domain 2; 1. DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase. DR InterPro; IPR010972; Beta-PGM. DR InterPro; IPR051600; Beta-PGM-like. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR023198; PGP-like_dom2. DR NCBIfam; TIGR01990; bPGM; 1. DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1. DR NCBIfam; TIGR02009; PGMB-YQAB-SF; 1. DR PANTHER; PTHR46193; 6-PHOSPHOGLUCONATE PHOSPHATASE; 1. DR PANTHER; PTHR46193:SF18; HEXITOL PHOSPHATASE B; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SFLD; SFLDF00046; beta-phosphoglucomutase; 1. DR SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1. DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SUPFAM; SSF56784; HAD-like; 1. 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 PDBsum; 8Q1C; -. DR PDBsum; 8Q1D; -. DR PDBsum; 8Q1E; -. DR PDBsum; 8Q1F; -. 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 /evidence="ECO:0000305|PubMed:15996095, FT ECO:0000305|PubMed:19154134" FT ACT_SITE 10 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000305|PubMed:15996095, FT ECO:0000305|PubMed:19154134" FT BINDING 8 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:12081483, FT ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149, FT ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:20164409, FT ECO:0007744|PDB:1LVH, ECO:0007744|PDB:1O03, FT ECO:0007744|PDB:1O08, ECO:0007744|PDB:1Z4N, FT ECO:0007744|PDB:1Z4O, ECO:0007744|PDB:1ZOL, FT ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6, FT ECO:0007744|PDB:2WHE" FT BINDING 10 FT /ligand="beta-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58247" FT /evidence="ECO:0000269|PubMed:20164409, FT ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:12081483, FT ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149, FT ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:20164409, FT ECO:0007744|PDB:1LVH, ECO:0007744|PDB:1O03, FT ECO:0007744|PDB:1O08, ECO:0007744|PDB:1Z4N, FT ECO:0007744|PDB:1Z4O, ECO:0007744|PDB:1ZOL, FT ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6, FT ECO:0007744|PDB:2WHE" FT BINDING 46 FT /ligand="beta-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58247" FT /evidence="ECO:0000269|PubMed:20164409, FT ECO:0000305|PubMed:12637673, ECO:0007744|PDB:1O03, FT ECO:0007744|PDB:1O08, ECO:0007744|PDB:2WF5, FT ECO:0007744|PDB:2WF6" FT BINDING 47 FT /ligand="beta-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58247" FT /evidence="ECO:0000269|PubMed:20164409, FT ECO:0000305|PubMed:12637673, ECO:0007744|PDB:1O03, FT ECO:0007744|PDB:1O08, ECO:0007744|PDB:2WF5, FT ECO:0007744|PDB:2WF6" FT BINDING 49 FT /ligand="beta-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58247" FT /evidence="ECO:0000269|PubMed:20164409, FT ECO:0000305|PubMed:12637673, ECO:0000305|PubMed:15826149, FT ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, FT ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O, FT ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6" FT BINDING 116 FT /ligand="beta-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58247" FT /evidence="ECO:0000269|PubMed:20164409, FT ECO:0000305|PubMed:12637673, ECO:0000305|PubMed:15826149, FT ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, FT ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O, FT ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6" FT BINDING 117 FT /ligand="beta-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58247" FT /evidence="ECO:0000269|PubMed:20164409, FT ECO:0000305|PubMed:12637673, ECO:0000305|PubMed:15826149, FT ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, FT ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O, FT ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6" FT BINDING 118 FT /ligand="beta-D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:58247" FT /evidence="ECO:0000269|PubMed:20164409, FT ECO:0000305|PubMed:12637673, ECO:0000305|PubMed:15826149, FT ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, FT ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O, FT ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6" FT BINDING 170 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:12081483, FT ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149, FT ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:20164409, FT ECO:0007744|PDB:1LVH, ECO:0007744|PDB:1O03, FT ECO:0007744|PDB:1O08, ECO:0007744|PDB:1Z4N, FT ECO:0007744|PDB:1Z4O, ECO:0007744|PDB:1ZOL, FT ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6, FT ECO:0007744|PDB:2WHE" 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 ECO:0000269|PubMed:19154134" FT MUTAGEN 8 FT /note="D->A,E: Inactive." FT /evidence="ECO:0000269|PubMed:15996095" FT MUTAGEN 10 FT /note="D->A,E,N,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 FT beta-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 catalytic efficiency." FT /evidence="ECO:0000269|PubMed:15005616" FT MUTAGEN 46 FT /note="G->A: 1'000'000-fold decrease in catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:15005616" FT MUTAGEN 46 FT /note="G->P: 100'000-fold decrease in catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:15005616" FT MUTAGEN 46 FT /note="G->V: 10'000-fold decrease in catalytic efficiency." FT /evidence="ECO:0000269|PubMed:15005616" FT MUTAGEN 49 FT /note="R->K: 1'000'000-fold decrease in catalytic FT efficiency." 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 FT beta-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:8Q1F" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 17..30 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 38..41 FT /evidence="ECO:0007829|PDB:8Q1F" FT TURN 42..46 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 49..59 FT /evidence="ECO:0007829|PDB:8Q1F" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:6HDG" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:6HDG" FT HELIX 66..83 FT /evidence="ECO:0007829|PDB:8Q1F" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 96..105 FT /evidence="ECO:0007829|PDB:8Q1F" FT STRAND 109..112 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 119..125 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:8Q1F" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:8Q1F" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:6YDJ" FT HELIX 149..157 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:8Q1F" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 172..181 FT /evidence="ECO:0007829|PDB:8Q1F" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 191..194 FT /evidence="ECO:0007829|PDB:8Q1F" FT STRAND 196..203 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:8Q1F" FT HELIX 209..219 FT /evidence="ECO:0007829|PDB:8Q1F" 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 //