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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)DescriptionActionsGraphical viewLength
Metal bindingi33Manganese 11 Publication1
Metal bindingi57Manganese 11 Publication1
Metal bindingi85Manganese 21 Publication1
Metal bindingi88Manganese 21 Publication1
Binding sitei119Substrate1 Publication1
Binding sitei210Substrate; via amide nitrogen1 Publication1
Metal bindingi213Manganese 21 Publication1

GO - Molecular functioni

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

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi29K → A: 2.4-fold increase in FBPase activity, and no effect on substrate affinity. 1 Publication1
Mutagenesisi57E → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi59E → A: 5.5-fold decrease in FBPase activity, and 1.4-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi61D → A: Great decrease in FBPase activity. 1 Publication1
Mutagenesisi85D → A: Great decrease in FBPase activity. 1 Publication1
Mutagenesisi88E → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi90T → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi119Y → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi164K → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi166R → A: Strong decrease in FBPase activity. 1 Publication1
Mutagenesisi186D → A: 5-fold decrease in FBPase activity, and 3-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi188D → A: Great decrease in FBPase activity. 1 Publication1
Mutagenesisi213E → A: Great decrease in FBPase activity. 1 Publication1
Mutagenesisi235R → A: Nearly no effect on FBPase activity, and 3-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi239K → A: 1.3-fold increase in FBPase activity, and 1.4-fold decrease in substrate affinity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002011001 – 336Fructose-1,6-bisphosphatase 1 class 2Add BLAST336

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 interactors.
IntActiP0A9C9. 6 interactors.
STRINGi511145.b3925.

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Helixi6 – 21Combined sources16
Turni22 – 25Combined sources4
Helixi29 – 44Combined sources16
Beta strandi50 – 58Combined sources9
Turni60 – 62Combined sources3
Beta strandi64 – 67Combined sources4
Beta strandi71 – 73Combined sources3
Beta strandi79 – 88Combined sources10
Helixi90 – 94Combined sources5
Beta strandi101 – 108Combined sources8
Beta strandi117 – 125Combined sources9
Helixi127 – 129Combined sources3
Helixi139 – 150Combined sources12
Helixi154 – 156Combined sources3
Beta strandi158 – 162Combined sources5
Helixi165 – 167Combined sources3
Helixi168 – 177Combined sources10
Beta strandi180 – 186Combined sources7
Helixi189 – 194Combined sources6
Beta strandi204 – 210Combined sources7
Helixi211 – 224Combined sources14
Beta strandi227 – 233Combined sources7
Helixi235 – 237Combined sources3
Helixi244 – 257Combined sources14
Turni258 – 260Combined sources3
Beta strandi265 – 268Combined sources4
Helixi269 – 272Combined sources4
Beta strandi278 – 286Combined sources9
Beta strandi289 – 291Combined sources3
Beta strandi295 – 297Combined sources3
Beta strandi300 – 309Combined sources10
Turni310 – 313Combined sources4
Beta strandi315 – 323Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9C9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni88 – 90Substrate binding1 Publication3
Regioni164 – 166Substrate binding1 Publication3
Regioni186 – 188Substrate binding1 Publication3

Sequence similaritiesi

Belongs to the FBPase class 2 family.Curated

Phylogenomic databases

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

Family and domain databases

CDDicd01516. FBPase_glpX. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260756. 11 interactors.
IntActiP0A9C9. 6 interactors.
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.
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

CDDicd01516. FBPase_glpX. 1 hit.
InterProiIPR004464. FBPase_class-2/SBPase.
[Graphical view]
PfamiPF03320. FBPase_glpX. 1 hit.
[Graphical view]
PIRSFiPIRSF004532. GlpX. 1 hit.
TIGRFAMsiTIGR00330. glpX. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 99 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.