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Protein

Fructose-1,6-bisphosphatase 1 class 2

Gene

glpX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Is likely to be involved in gluconeogenesis during growth on glycerol. Also displays a low activity toward glucose 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate, fructose 2,6-bisphosphate, or fructose 1-phosphate.2 Publications

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.2 Publications

Cofactori

Mn2+2 PublicationsNote: Manganese. Mg2+, Co2+, Ni2+, Ca2+, Cu2+ and Zn2+ cannot support activity.2 Publications

Enzyme regulationi

Competitively inhibited by low concentrations of phosphate (IC50 3.0 mM) and is also sensitive to Li+ (IC50 70 mM). Slightly activated by KCl.1 Publication

Kineticsi

The catalytic efficiency of GlpX is 3-fold higher than that of YggF, the other FBPase class 2 in E.coli.

  1. KM=35 µM for fructose 1,6-bisphosphate (at pH 7.7 and room temperature)2 Publications
  2. KM=70 µM for fructose 1,6-bisphosphate (at pH 9.0 and 37 degrees Celsius)2 Publications
  3. KM=0.6 mM for Mn2+ (at pH 9.0 and 37 degrees Celsius)2 Publications
  1. Vmax=3.3 µmol/min/mg enzyme (at pH 7.7 and room temperature)2 Publications
  2. Vmax=8.8 µmol/min/mg enzyme (at pH 9.0 and 37 degrees Celsius)2 Publications

pH dependencei

Optimum pH is 7.5-8.1 Publication

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi33 – 331Manganese 1
Metal bindingi57 – 571Manganese 1
Metal bindingi85 – 851Manganese 2
Metal bindingi88 – 881Manganese 2
Binding sitei119 – 1191Substrate
Binding sitei210 – 2101Substrate; via amide nitrogen
Metal bindingi213 – 2131Manganese 2

GO - Molecular functioni

  • fructose 1,6-bisphosphate 1-phosphatase activity Source: EcoCyc
  • manganese ion binding Source: EcoCyc

GO - Biological processi

  • dephosphorylation Source: GOC
  • gluconeogenesis Source: UniProtKB-UniPathway
  • glycerol metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11517-MONOMER.
ECOL316407:JW3896-MONOMER.
MetaCyc:EG11517-MONOMER.
BRENDAi3.1.3.11. 2026.
SABIO-RKP0A9C9.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase 1 class 2 (EC:3.1.3.11)
Short name:
FBPase 1 class 2
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1 class 2
Gene namesi
Name:glpX
Ordered Locus Names:b3925, JW3896
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11517. glpX.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene grow normally on gluconeogenic substrates (succinate or glycerol).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291K → A: 2.4-fold increase in FBPase activity, and no effect on substrate affinity. 1 Publication
Mutagenesisi57 – 571E → A: Strong decrease in FBPase activity. 1 Publication
Mutagenesisi59 – 591E → A: 5.5-fold decrease in FBPase activity, and 1.4-fold decrease in substrate affinity. 1 Publication
Mutagenesisi61 – 611D → A: Great decrease in FBPase activity. 1 Publication
Mutagenesisi85 – 851D → A: Great decrease in FBPase activity. 1 Publication
Mutagenesisi88 – 881E → A: Strong decrease in FBPase activity. 1 Publication
Mutagenesisi90 – 901T → A: Strong decrease in FBPase activity. 1 Publication
Mutagenesisi119 – 1191Y → A: Strong decrease in FBPase activity. 1 Publication
Mutagenesisi164 – 1641K → A: Strong decrease in FBPase activity. 1 Publication
Mutagenesisi166 – 1661R → A: Strong decrease in FBPase activity. 1 Publication
Mutagenesisi186 – 1861D → A: 5-fold decrease in FBPase activity, and 3-fold decrease in substrate affinity. 1 Publication
Mutagenesisi188 – 1881D → A: Great decrease in FBPase activity. 1 Publication
Mutagenesisi213 – 2131E → A: Great decrease in FBPase activity. 1 Publication
Mutagenesisi235 – 2351R → A: Nearly no effect on FBPase activity, and 3-fold decrease in substrate affinity. 1 Publication
Mutagenesisi239 – 2391K → A: 1.3-fold increase in FBPase activity, and 1.4-fold decrease in substrate affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Fructose-1,6-bisphosphatase 1 class 2PRO_0000201100Add
BLAST

Proteomic databases

EPDiP0A9C9.
PaxDbiP0A9C9.
PRIDEiP0A9C9.

Expressioni

Inductioni

By glycerol and sn-glycerol-3-phosphate.1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi4260756. 11 interactions.
IntActiP0A9C9. 6 interactions.
STRINGi511145.b3925.

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi6 – 2116Combined sources
Turni22 – 254Combined sources
Helixi29 – 4416Combined sources
Beta strandi50 – 589Combined sources
Turni60 – 623Combined sources
Beta strandi64 – 674Combined sources
Beta strandi71 – 733Combined sources
Beta strandi79 – 8810Combined sources
Helixi90 – 945Combined sources
Beta strandi101 – 1088Combined sources
Beta strandi117 – 1259Combined sources
Helixi127 – 1293Combined sources
Helixi139 – 15012Combined sources
Helixi154 – 1563Combined sources
Beta strandi158 – 1625Combined sources
Helixi165 – 1673Combined sources
Helixi168 – 17710Combined sources
Beta strandi180 – 1867Combined sources
Helixi189 – 1946Combined sources
Beta strandi204 – 2107Combined sources
Helixi211 – 22414Combined sources
Beta strandi227 – 2337Combined sources
Helixi235 – 2373Combined sources
Helixi244 – 25714Combined sources
Turni258 – 2603Combined sources
Beta strandi265 – 2684Combined sources
Helixi269 – 2724Combined sources
Beta strandi278 – 2869Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi300 – 30910Combined sources
Turni310 – 3134Combined sources
Beta strandi315 – 3239Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI9X-ray2.00A1-336[»]
2R8TX-ray2.30A1-336[»]
3BIGX-ray1.85A1-336[»]
3BIHX-ray2.10A1-336[»]
3D1RX-ray1.85A1-336[»]
ProteinModelPortaliP0A9C9.
SMRiP0A9C9. Positions 1-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9C9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 903Substrate binding
Regioni164 – 1663Substrate binding
Regioni186 – 1883Substrate binding

Sequence similaritiesi

Belongs to the FBPase class 2 family.Curated

Phylogenomic databases

eggNOGiENOG4105CBT. Bacteria.
COG1494. LUCA.
HOGENOMiHOG000241252.
InParanoidiP0A9C9.
KOiK02446.
OMAiVIQGRLW.
OrthoDBiEOG6R87CH.
PhylomeDBiP0A9C9.

Family and domain databases

InterProiIPR004464. FBPase_class-2/SBPase.
[Graphical view]
PfamiPF03320. FBPase_glpX. 1 hit.
[Graphical view]
PIRSFiPIRSF004532. GlpX. 1 hit.
TIGRFAMsiTIGR00330. glpX. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A9C9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRELAIEFS RVTESAALAG YKWLGRGDKN TADGAAVNAM RIMLNQVNID
60 70 80 90 100
GTIVIGEGEI DEAPMLYIGE KVGTGRGDAV DIAVDPIEGT RMTAMGQANA
110 120 130 140 150
LAVLAVGDKG CFLNAPDMYM EKLIVGPGAK GTIDLNLPLA DNLRNVAAAL
160 170 180 190 200
GKPLSELTVT ILAKPRHDAV IAEMQQLGVR VFAIPDGDVA ASILTCMPDS
210 220 230 240 250
EVDVLYGIGG APEGVVSAAV IRALDGDMNG RLLARHDVKG DNEENRRIGE
260 270 280 290 300
QELARCKAMG IEAGKVLRLG DMARSDNVIF SATGITKGDL LEGISRKGNI
310 320 330
ATTETLLIRG KSRTIRRIQS IHYLDRKDPE MQVHIL
Length:336
Mass (Da):35,852
Last modified:July 19, 2005 - v1
Checksum:iDEC2A477E5C4062E
GO

Sequence cautioni

The sequence M19644 differs from that shown.The C-terminal part of glpX was incorrectly assigned as being part of mvrA.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11767 Genomic DNA. Translation: CAA77814.1.
L19201 Genomic DNA. Translation: AAB03057.1.
U00096 Genomic DNA. Translation: AAC76907.1.
AP009048 Genomic DNA. Translation: BAE77385.1.
M19644 Genomic DNA. No translation available.
PIRiA45248.
RefSeqiNP_418360.1. NC_000913.3.
WP_001250644.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76907; AAC76907; b3925.
BAE77385; BAE77385; BAE77385.
GeneIDi948424.
KEGGiecj:JW3896.
eco:b3925.
PATRICi32123363. VBIEscCol129921_4042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11767 Genomic DNA. Translation: CAA77814.1.
L19201 Genomic DNA. Translation: AAB03057.1.
U00096 Genomic DNA. Translation: AAC76907.1.
AP009048 Genomic DNA. Translation: BAE77385.1.
M19644 Genomic DNA. No translation available.
PIRiA45248.
RefSeqiNP_418360.1. NC_000913.3.
WP_001250644.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI9X-ray2.00A1-336[»]
2R8TX-ray2.30A1-336[»]
3BIGX-ray1.85A1-336[»]
3BIHX-ray2.10A1-336[»]
3D1RX-ray1.85A1-336[»]
ProteinModelPortaliP0A9C9.
SMRiP0A9C9. Positions 1-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260756. 11 interactions.
IntActiP0A9C9. 6 interactions.
STRINGi511145.b3925.

Proteomic databases

EPDiP0A9C9.
PaxDbiP0A9C9.
PRIDEiP0A9C9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76907; AAC76907; b3925.
BAE77385; BAE77385; BAE77385.
GeneIDi948424.
KEGGiecj:JW3896.
eco:b3925.
PATRICi32123363. VBIEscCol129921_4042.

Organism-specific databases

EchoBASEiEB1479.
EcoGeneiEG11517. glpX.

Phylogenomic databases

eggNOGiENOG4105CBT. Bacteria.
COG1494. LUCA.
HOGENOMiHOG000241252.
InParanoidiP0A9C9.
KOiK02446.
OMAiVIQGRLW.
OrthoDBiEOG6R87CH.
PhylomeDBiP0A9C9.

Enzyme and pathway databases

UniPathwayiUPA00138.
BioCyciEcoCyc:EG11517-MONOMER.
ECOL316407:JW3896-MONOMER.
MetaCyc:EG11517-MONOMER.
BRENDAi3.1.3.11. 2026.
SABIO-RKP0A9C9.

Miscellaneous databases

EvolutionaryTraceiP0A9C9.
PROiP0A9C9.

Family and domain databases

InterProiIPR004464. FBPase_class-2/SBPase.
[Graphical view]
PfamiPF03320. FBPase_glpX. 1 hit.
[Graphical view]
PIRSFiPIRSF004532. GlpX. 1 hit.
TIGRFAMsiTIGR00330. glpX. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri."
    Truniger V., Boos W., Sweet G.
    J. Bacteriol. 174:6981-6991(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  2. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Isolation and characterization of methyl viologen-sensitive mutants of Escherichia coli K-12."
    Morimyo M.
    J. Bacteriol. 170:2136-2142(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-336.
    Strain: K12.
  6. "Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli."
    Donahue J.L., Bownas J.L., Niehaus W.G., Larson T.J.
    J. Bacteriol. 182:5624-5627(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, KINETIC PARAMETERS, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Structural and biochemical characterization of the type II fructose-1,6-bisphosphatase GlpX from Escherichia coli."
    Brown G., Singer A., Lunin V.V., Proudfoot M., Skarina T., Flick R., Kochinyan S., Sanishvili R., Joachimiak A., Edwards A.M., Savchenko A., Yakunin A.F.
    J. Biol. Chem. 284:3784-3792(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF APOENZYME AND MUTANT ALA-61 IN COMPLEXES WITH SUBSTRATE; METAL IONS AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM, MUTAGENESIS OF LYS-29; GLU-57; GLU-59; ASP-61; ASP-85; GLU-88; THR-90; TYR-119; LYS-164; ARG-166; ASP-186; ASP-188; GLU-213; ARG-235 AND LYS-239.
    Strain: K12 / DH5-alpha.

Entry informationi

Entry nameiGLPX_ECOLI
AccessioniPrimary (citable) accession number: P0A9C9
Secondary accession number(s): P11007
, P28860, P28900, Q2M8M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 16, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

E.coli K12 also possesses a FBPase class 1 (Fbp), which is the primary FBPase in E.coli and probably represents the main gluconeogenic FBPase.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.