GLPX2_ECOLI
ID GLPX2_ECOLI Reviewed; 321 AA.
AC P21437; P39837; Q2M9R2;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Fructose-1,6-bisphosphatase 2 class 2;
DE Short=FBPase 2 class 2;
DE EC=3.1.3.11;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 2 class 2;
GN Name=yggF; Synonyms=yggK; OrderedLocusNames=b2930, JW2897;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-321.
RX PubMed=2546007; DOI=10.1111/j.1365-2958.1989.tb00221.x;
RA Alefounder P.R., Perham R.N.;
RT "Identification, molecular cloning and sequence analysis of a gene cluster
RT encoding the class II fructose 1,6-bisphosphate aldolase, 3-
RT phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate
RT dehydrogenase of Escherichia coli.";
RL Mol. Microbiol. 3:723-732(1989).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=K12;
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. Also displays a low activity toward glucose 1,6-
CC bisphosphate, and no activity against ribulose 1,5-bisphosphate,
CC fructose 2,6-bisphosphate, or fructose 1-phosphate.
CC {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:19073594};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={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:19073594};
CC -!- ACTIVITY REGULATION: Competitively inhibited by low concentrations of
CC phosphate (IC50 of 1.2 mM) and is also sensitive to Li(+) (IC50 of 15.8
CC mM). Also inhibited by 1 mM ATP or 50 mM KCl (60% and 20% residual
CC activity, respectively). Slightly activated (40-50%) by the addition of
CC 1 mM dithiothreitol in vitro. {ECO:0000269|PubMed:19073594}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:19073594};
CC KM=1 mM for Mn(2+) {ECO:0000269|PubMed:19073594};
CC Vmax=4.0 umol/min/mg enzyme {ECO:0000269|PubMed:19073594};
CC Note=The catalytic efficiency of YggF is 3-fold lower than that of
CC GlpX, the other FBPase class 2 in E.coli.;
CC pH dependence:
CC Optimum pH is 7.5-8. {ECO:0000269|PubMed:19073594};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19073594}.
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=CAA32600.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U28377; AAA69097.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75967.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76994.1; -; Genomic_DNA.
DR EMBL; X14436; CAA32600.1; ALT_FRAME; Genomic_DNA.
DR PIR; A65078; QQEC15.
DR RefSeq; NP_417405.1; NC_000913.3.
DR RefSeq; WP_000987283.1; NZ_SSZK01000003.1.
DR AlphaFoldDB; P21437; -.
DR SMR; P21437; -.
DR BioGRID; 4262334; 128.
DR IntAct; P21437; 6.
DR STRING; 511145.b2930; -.
DR PaxDb; P21437; -.
DR PRIDE; P21437; -.
DR EnsemblBacteria; AAC75967; AAC75967; b2930.
DR EnsemblBacteria; BAE76994; BAE76994; BAE76994.
DR GeneID; 947410; -.
DR KEGG; ecj:JW2897; -.
DR KEGG; eco:b2930; -.
DR PATRIC; fig|1411691.4.peg.3802; -.
DR EchoBASE; EB1226; -.
DR eggNOG; COG1494; Bacteria.
DR HOGENOM; CLU_054938_0_0_6; -.
DR InParanoid; P21437; -.
DR OMA; DRTCNII; -.
DR PhylomeDB; P21437; -.
DR BioCyc; EcoCyc:EG11245-MON; -.
DR BioCyc; MetaCyc:EG11245-MON; -.
DR BRENDA; 3.1.3.11; 2026.
DR PRO; PR:P21437; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 Carbohydrate metabolism; Hydrolase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..321
FT /note="Fructose-1,6-bisphosphatase 2 class 2"
FT /id="PRO_0000201104"
FT BINDING 32
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 87..89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163..165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185..187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 182..186
FT /note="ALPDG -> CPAGC (in Ref. 3; CAA32600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 34323 MW; AB41094DAE321E50 CRC64;
MMSLAWPLFR VTEQAALAAW PQTGCGDKNK IDGLAVTAMR QALNDVAFRG RVVIGEGEID
HAPMLWIGEE VGKGDGPEVD IAVDPIEGTR MVAMGQSNAL AVMAFAPRDS LLHAPDMYMK
KLVVNRLAAG AIDLSLPLTD NLRNVAKALG KPLDKLRMVT LDKPRLSAAI EEATQLGVKV
FALPDGDVAA SVLTCWQDNP YDVMYTIGGA PEGVISACAV KALGGDMQAE LIDFCQAKGD
YTENRQIAEQ ERKRCKAMGV DVNRVYSLDE LVRGNDILFS ATGVTGGELV NGIQQTANGV
RTQTLLIGGA DQTCNIIDSL H
