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Protein

Fructose-1,6-bisphosphatase 2 class 2

Gene

yggF

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. 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.1 Publication

Catalytic activityi

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

Cofactori

Mn2+1 PublicationNote: Manganese. Mg2+, Co2+, Ni2+, Ca2+, Cu2+ and Zn2+ cannot support activity.1 Publication

Enzyme regulationi

Competitively inhibited by low concentrations of phosphate (IC50 of 1.2 mM) and is also sensitive to Li+ (IC50 of 15.8 mM). Also inhibited by 1 mM ATP or 50 mM KCl (60% and 20% residual activity, respectively). Slightly activated (40-50%) by the addition of 1 mM dithiothreitol in vitro.1 Publication

Kineticsi

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

  1. KM=100 µM for fructose 1,6-bisphosphate1 Publication
  2. KM=1 mM for Mn2+1 Publication
  1. Vmax=4.0 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.5-8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi32Manganese 1By similarity1
Metal bindingi56Manganese 1By similarity1
Metal bindingi84Manganese 2By similarity1
Metal bindingi87Manganese 2By similarity1
Binding sitei118SubstrateBy similarity1
Binding sitei209Substrate; via amide nitrogenBy similarity1
Metal bindingi212Manganese 2By similarity1

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:EG11245-MONOMER.
ECOL316407:JW2897-MONOMER.
MetaCyc:EG11245-MONOMER.
BRENDAi3.1.3.11. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-1,6-bisphosphatase 2 class 2 (EC:3.1.3.11)
Short name:
FBPase 2 class 2
Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase 2 class 2
Gene namesi
Name:yggF
Synonyms:yggK
Ordered Locus Names:b2930, JW2897
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11245. yggF.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002011041 – 321Fructose-1,6-bisphosphatase 2 class 2Add BLAST321

Proteomic databases

PaxDbiP21437.
PRIDEiP21437.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262334. 128 interactors.
IntActiP21437. 6 interactors.
STRINGi511145.b2930.

Structurei

3D structure databases

ProteinModelPortaliP21437.
SMRiP21437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni87 – 89Substrate bindingBy similarity3
Regioni163 – 165Substrate bindingBy similarity3
Regioni185 – 187Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the FBPase class 2 family.Curated

Phylogenomic databases

eggNOGiENOG4108Q8A. Bacteria.
COG1494. LUCA.
HOGENOMiHOG000241252.
InParanoidiP21437.
OMAiRTCNIID.
PhylomeDBiP21437.

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.

P21437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSLAWPLFR VTEQAALAAW PQTGCGDKNK IDGLAVTAMR QALNDVAFRG
60 70 80 90 100
RVVIGEGEID HAPMLWIGEE VGKGDGPEVD IAVDPIEGTR MVAMGQSNAL
110 120 130 140 150
AVMAFAPRDS LLHAPDMYMK KLVVNRLAAG AIDLSLPLTD NLRNVAKALG
160 170 180 190 200
KPLDKLRMVT LDKPRLSAAI EEATQLGVKV FALPDGDVAA SVLTCWQDNP
210 220 230 240 250
YDVMYTIGGA PEGVISACAV KALGGDMQAE LIDFCQAKGD YTENRQIAEQ
260 270 280 290 300
ERKRCKAMGV DVNRVYSLDE LVRGNDILFS ATGVTGGELV NGIQQTANGV
310 320
RTQTLLIGGA DQTCNIIDSL H
Length:321
Mass (Da):34,323
Last modified:November 1, 1995 - v2
Checksum:iAB41094DAE321E50
GO

Sequence cautioni

The sequence CAA32600 differs from that shown. Reason: Frameshift at position 219.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti182 – 186ALPDG → CPAGC in CAA32600 (PubMed:2546007).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28377 Genomic DNA. Translation: AAA69097.1.
U00096 Genomic DNA. Translation: AAC75967.1.
AP009048 Genomic DNA. Translation: BAE76994.1.
X14436 Genomic DNA. Translation: CAA32600.1. Frameshift.
PIRiA65078. QQEC15.
RefSeqiNP_417405.1. NC_000913.3.
WP_000987283.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75967; AAC75967; b2930.
BAE76994; BAE76994; BAE76994.
GeneIDi947410.
KEGGiecj:JW2897.
eco:b2930.
PATRICi32121274. VBIEscCol129921_3025.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28377 Genomic DNA. Translation: AAA69097.1.
U00096 Genomic DNA. Translation: AAC75967.1.
AP009048 Genomic DNA. Translation: BAE76994.1.
X14436 Genomic DNA. Translation: CAA32600.1. Frameshift.
PIRiA65078. QQEC15.
RefSeqiNP_417405.1. NC_000913.3.
WP_000987283.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP21437.
SMRiP21437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262334. 128 interactors.
IntActiP21437. 6 interactors.
STRINGi511145.b2930.

Proteomic databases

PaxDbiP21437.
PRIDEiP21437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75967; AAC75967; b2930.
BAE76994; BAE76994; BAE76994.
GeneIDi947410.
KEGGiecj:JW2897.
eco:b2930.
PATRICi32121274. VBIEscCol129921_3025.

Organism-specific databases

EchoBASEiEB1226.
EcoGeneiEG11245. yggF.

Phylogenomic databases

eggNOGiENOG4108Q8A. Bacteria.
COG1494. LUCA.
HOGENOMiHOG000241252.
InParanoidiP21437.
OMAiRTCNIID.
PhylomeDBiP21437.

Enzyme and pathway databases

BioCyciEcoCyc:EG11245-MONOMER.
ECOL316407:JW2897-MONOMER.
MetaCyc:EG11245-MONOMER.
BRENDAi3.1.3.11. 2026.

Miscellaneous databases

PROiP21437.

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 nameiGLPX2_ECOLI
AccessioniPrimary (citable) accession number: P21437
Secondary accession number(s): P39837, Q2M9R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 121 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.