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Protein

Fructose-1,6-bisphosphatase 2 class 2

Gene

yggF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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.

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

Keywordsi

Molecular functionHydrolase
Biological processCarbohydrate metabolism
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11245-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

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
STRINGi316385.ECDH10B_3105

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
OMAiDRTCNII
PhylomeDBiP21437

Family and domain databases

CDDicd01516 FBPase_glpX, 1 hit
InterProiView protein in InterPro
IPR004464 FBPase_class-2/SBPase
PANTHERiPTHR30447 PTHR30447, 1 hit
PfamiView protein in Pfam
PF03320 FBPase_glpX, 1 hit
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
PATRICifig|1411691.4.peg.3802

Similar proteinsi

Entry informationi

Entry nameiGLPX2_ECOLI
AccessioniPrimary (citable) accession number: P21437
Secondary accession number(s): P39837, Q2M9R2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1995
Last modified: March 28, 2018
This is version 127 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health