GLPX_ECOLI
ID GLPX_ECOLI Reviewed; 336 AA.
AC P0A9C9; P11007; P28860; P28900; Q2M8M1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Fructose-1,6-bisphosphatase 1 class 2;
DE Short=FBPase 1 class 2;
DE EC=3.1.3.11;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1 class 2;
GN Name=glpX; OrderedLocusNames=b3925, JW3896;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=1400248; DOI=10.1128/jb.174.21.6981-6991.1992;
RA Truniger V., Boos W., Sweet G.;
RT "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella
RT flexneri.";
RL J. Bacteriol. 174:6981-6991(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-336.
RC STRAIN=K12;
RX PubMed=2834327; DOI=10.1128/jb.170.5.2136-2142.1988;
RA Morimyo M.;
RT "Isolation and characterization of methyl viologen-sensitive mutants of
RT Escherichia coli K-12.";
RL J. Bacteriol. 170:2136-2142(1988).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, KINETIC PARAMETERS, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=10986273; DOI=10.1128/jb.182.19.5624-5627.2000;
RA Donahue J.L., Bownas J.L., Niehaus W.G., Larson T.J.;
RT "Purification and characterization of glpX-encoded fructose 1, 6-
RT bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of
RT Escherichia coli.";
RL J. Bacteriol. 182:5624-5627(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF APOENZYME AND MUTANT ALA-61 IN
RP COMPLEXES WITH SUBSTRATE; METAL IONS AND PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM, AND MUTAGENESIS
RP OF LYS-29; GLU-57; GLU-59; ASP-61; ASP-85; GLU-88; THR-90; TYR-119;
RP LYS-164; ARG-166; ASP-186; ASP-188; GLU-213; ARG-235 AND LYS-239.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=19073594; DOI=10.1074/jbc.m808186200;
RA Brown G., Singer A., Lunin V.V., Proudfoot M., Skarina T., Flick R.,
RA Kochinyan S., Sanishvili R., Joachimiak A., Edwards A.M., Savchenko A.,
RA Yakunin A.F.;
RT "Structural and biochemical characterization of the type II fructose-1,6-
RT bisphosphatase GlpX from Escherichia coli.";
RL J. Biol. Chem. 284:3784-3792(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate. Is likely to be involved in gluconeogenesis
CC during growth on glycerol. Also displays a low activity toward glucose
CC 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate,
CC fructose 2,6-bisphosphate, or fructose 1-phosphate.
CC {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594};
CC Note=Manganese. Mg(2+), Co(2+), Ni(2+), Ca(2+), Cu(2+) and Zn(2+)
CC cannot support activity. {ECO:0000269|PubMed:10986273,
CC ECO:0000269|PubMed:19073594};
CC -!- ACTIVITY REGULATION: Competitively inhibited by low concentrations of
CC phosphate (IC50 3.0 mM) and is also sensitive to Li(+) (IC50 70 mM).
CC Slightly activated by KCl. {ECO:0000269|PubMed:19073594}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=35 uM for fructose 1,6-bisphosphate (at pH 7.7 and room
CC temperature) {ECO:0000269|PubMed:10986273,
CC ECO:0000269|PubMed:19073594};
CC KM=70 uM for fructose 1,6-bisphosphate (at pH 9.0 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594};
CC KM=0.6 mM for Mn(2+) (at pH 9.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594};
CC Vmax=3.3 umol/min/mg enzyme (at pH 7.7 and room temperature)
CC {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594};
CC Vmax=8.8 umol/min/mg enzyme (at pH 9.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594};
CC Note=The catalytic efficiency of GlpX is 3-fold higher than that of
CC YggF, the other FBPase class 2 in E.coli.;
CC pH dependence:
CC Optimum pH is 7.5-8. {ECO:0000269|PubMed:19073594};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10986273,
CC ECO:0000269|PubMed:19073594}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By glycerol and sn-glycerol-3-phosphate.
CC {ECO:0000269|PubMed:1400248}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow normally on
CC gluconeogenic substrates (succinate or glycerol).
CC {ECO:0000269|PubMed:10986273}.
CC -!- MISCELLANEOUS: E.coli K12 also possesses a FBPase class 1 (Fbp), which
CC is the primary FBPase in E.coli and probably represents the main
CC gluconeogenic FBPase.
CC -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M19644; Type=Miscellaneous discrepancy; Note=The C-terminal part of glpX was incorrectly assigned as being part of mvrA.; Evidence={ECO:0000305};
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DR EMBL; Z11767; CAA77814.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03057.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76907.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77385.1; -; Genomic_DNA.
DR EMBL; M19644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A45248; A45248.
DR RefSeq; NP_418360.1; NC_000913.3.
DR RefSeq; WP_001250644.1; NZ_STEB01000017.1.
DR PDB; 1NI9; X-ray; 2.00 A; A=1-336.
DR PDB; 2R8T; X-ray; 2.30 A; A=1-336.
DR PDB; 3BIG; X-ray; 1.85 A; A=1-336.
DR PDB; 3BIH; X-ray; 2.10 A; A=1-336.
DR PDB; 3D1R; X-ray; 1.85 A; A=1-336.
DR PDBsum; 1NI9; -.
DR PDBsum; 2R8T; -.
DR PDBsum; 3BIG; -.
DR PDBsum; 3BIH; -.
DR PDBsum; 3D1R; -.
DR AlphaFoldDB; P0A9C9; -.
DR SMR; P0A9C9; -.
DR BioGRID; 4260756; 16.
DR BioGRID; 852721; 1.
DR IntAct; P0A9C9; 6.
DR STRING; 511145.b3925; -.
DR jPOST; P0A9C9; -.
DR PaxDb; P0A9C9; -.
DR PRIDE; P0A9C9; -.
DR EnsemblBacteria; AAC76907; AAC76907; b3925.
DR EnsemblBacteria; BAE77385; BAE77385; BAE77385.
DR GeneID; 67417564; -.
DR GeneID; 948424; -.
DR KEGG; ecj:JW3896; -.
DR KEGG; eco:b3925; -.
DR PATRIC; fig|1411691.4.peg.2780; -.
DR EchoBASE; EB1479; -.
DR eggNOG; COG1494; Bacteria.
DR HOGENOM; CLU_054938_0_0_6; -.
DR InParanoid; P0A9C9; -.
DR OMA; AVFYMDK; -.
DR PhylomeDB; P0A9C9; -.
DR BioCyc; EcoCyc:EG11517-MON; -.
DR BioCyc; MetaCyc:EG11517-MON; -.
DR BRENDA; 3.1.3.11; 2026.
DR SABIO-RK; P0A9C9; -.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; P0A9C9; -.
DR PRO; PR:P0A9C9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR CDD; cd01516; FBPase_glpX; 1.
DR InterPro; IPR004464; FBPase_class-2/SBPase.
DR PANTHER; PTHR30447; PTHR30447; 1.
DR Pfam; PF03320; FBPase_glpX; 1.
DR PIRSF; PIRSF004532; GlpX; 1.
DR TIGRFAMs; TIGR00330; glpX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..336
FT /note="Fructose-1,6-bisphosphatase 1 class 2"
FT /id="PRO_0000201100"
FT BINDING 33
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:19073594"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:19073594"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:19073594"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19073594"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:19073594"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19073594"
FT BINDING 164..166
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19073594"
FT BINDING 186..188
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19073594"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19073594"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:19073594"
FT MUTAGEN 29
FT /note="K->A: 2.4-fold increase in FBPase activity, and no
FT effect on substrate affinity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 57
FT /note="E->A: Strong decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 59
FT /note="E->A: 5.5-fold decrease in FBPase activity, and 1.4-
FT fold decrease in substrate affinity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 61
FT /note="D->A: Great decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 85
FT /note="D->A: Great decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 88
FT /note="E->A: Strong decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 90
FT /note="T->A: Strong decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 119
FT /note="Y->A: Strong decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 164
FT /note="K->A: Strong decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 166
FT /note="R->A: Strong decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 186
FT /note="D->A: 5-fold decrease in FBPase activity, and 3-fold
FT decrease in substrate affinity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 188
FT /note="D->A: Great decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 213
FT /note="E->A: Great decrease in FBPase activity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 235
FT /note="R->A: Nearly no effect on FBPase activity, and 3-
FT fold decrease in substrate affinity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT MUTAGEN 239
FT /note="K->A: 1.3-fold increase in FBPase activity, and 1.4-
FT fold decrease in substrate affinity."
FT /evidence="ECO:0000269|PubMed:19073594"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:3BIG"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:3BIG"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:3BIG"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3BIG"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3BIG"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:3BIG"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:1NI9"
FT STRAND 315..323
FT /evidence="ECO:0007829|PDB:3BIG"
SQ SEQUENCE 336 AA; 35852 MW; DEC2A477E5C4062E CRC64;
MRRELAIEFS RVTESAALAG YKWLGRGDKN TADGAAVNAM RIMLNQVNID GTIVIGEGEI
DEAPMLYIGE KVGTGRGDAV DIAVDPIEGT RMTAMGQANA LAVLAVGDKG CFLNAPDMYM
EKLIVGPGAK GTIDLNLPLA DNLRNVAAAL GKPLSELTVT ILAKPRHDAV IAEMQQLGVR
VFAIPDGDVA ASILTCMPDS EVDVLYGIGG APEGVVSAAV IRALDGDMNG RLLARHDVKG
DNEENRRIGE QELARCKAMG IEAGKVLRLG DMARSDNVIF SATGITKGDL LEGISRKGNI
ATTETLLIRG KSRTIRRIQS IHYLDRKDPE MQVHIL
