P0A993 (F16PA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fructose-1,6-bisphosphatase class 1
Short name=FBPase class 1
EC=3.1.3.11

Alternative name(s):
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1

Gene names

Name:	fbp
Synonyms:	fdp
Ordered Locus Names:	b4232, JW4191

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate. HAMAP-Rule MF_01855
Cofactor	Binds 2 magnesium ions per subunit. Ref.7 Ref.9
Enzyme regulation	Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. Activated by three-carbon carboxylic acids, phosphorylated three-carbon carboxylic acids and sulfate. Strongly activated by phosphoenolpyruvate and citrate. Inhibited by AMP, which affects the turnover of bound substrate and not the affinity for substrate. Allosterically inhibited by glucose 6-phosphate. AMP and glucose 6-phosphate act synergistically as allosteric inhibitors. Phosphoenolpyruvate antagonizes inhibition by AMP and glucose 6-phosphate. Fructose 2,6-bisphosphate acts as competitive inhibitor. Ref.7 Ref.8 Ref.9 Ref.10
Pathway	Carbohydrate biosynthesis; gluconeogenesis. HAMAP-Rule MF_01855
Subunit structure	Homotetramer. Phosphoenolpyruvate stabilizes the homotetramer. Ref.7 Ref.8 Ref.9
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_01855.
Sequence similarities	Belongs to the FBPase class 1 family.
Biophysicochemical properties	Kinetic parameters: KM=1.7 µM for fructose 1,6-biphosphate Ref.7

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Inferred from mutant phenotype PubMed 4284917. Source: EcoCyc reductive pentose-phosphate cycle Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from direct assay PubMed 11825604. Source: EcoCyc magnesium ion binding Inferred from electronic annotation. Source: HAMAP nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 332

332

Fructose-1,6-bisphosphatase class 1 HAMAP-Rule MF_01855

PRO_0000200492

Regions

Nucleotide binding

19 – 23

5

AMP HAMAP-Rule MF_01855

Nucleotide binding

104 – 105

2

AMP HAMAP-Rule MF_01855

Region

3 – 5

3

Allosteric activator binding HAMAP-Rule MF_01855

Region

113 – 116

4

Substrate binding HAMAP-Rule MF_01855

Region

257 – 259

3

Substrate binding HAMAP-Rule MF_01855

Sites

Metal binding

89

1

Magnesium 1

Metal binding

110

1

Magnesium 1

Metal binding

110

1

Magnesium 2

Metal binding

112

1

Magnesium 1; via carbonyl oxygen

Metal binding

113

1

Magnesium 2

Metal binding

275

1

Magnesium 2

Binding site

30

1

Allosteric activator

Binding site

187

1

Allosteric activator; via amide nitrogen

Binding site

206

1

Substrate

Binding site

222

1

Allosteric inhibitor glucose-6-phosphate

Binding site

225

1

Allosteric inhibitor glucose-6-phosphate

Binding site

239

1

Substrate

Binding site

269

1

Substrate

Secondary structure

1

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332

Helix Strand Turn

Details...

Helix

4 – 10

7

Turn

11 – 14

4

Helix

15 – 17

3

Helix

19 – 40

22

Turn

41 – 48

8

Beta strand

50 – 55

6

Beta strand

61 – 63

3

Helix

65 – 79

15

Beta strand

83 – 88

6

Beta strand

105 – 113

9

Helix

115 – 120

6

Beta strand

124 – 132

9

Helix

143 – 146

4

Helix

150 – 152

3

Beta strand

154 – 173

20

Beta strand

175 – 180

6

Turn

182 – 184

3

Beta strand

186 – 194

9

Beta strand

202 – 204

3

Helix

207 – 212

6

Helix

215 – 224

10

Helix

229 – 231

3

Helix

243 – 253

11

Beta strand

256 – 259

4

Beta strand

263 – 265

3

Beta strand

269 – 271

3

Turn

272 – 275

4

Helix

276 – 285

10

Beta strand

289 – 296

8

Helix

297 – 299

3

Beta strand

311 – 315

5

Helix

316 – 328

13

Sequences

	Sequence		Length	Mass (Da)
	P0A993 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 4F0FC8109491D78F	FASTA	332	36,834
	10 20 30 40 50 60 MKTLGEFIVE KQHEFSHATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG ASGAENVQGE 70 80 90 100 110 120 VQQKLDLFAN EKLKAALKAR DIVAGIASEE EDEIVVFEGC EHAKYVVLMD PLDGSSNIDV 130 140 150 160 170 180 NVSVGTIFSI YRRVTPVGTP VTEEDFLQPG NKQVAAGYVV YGSSTMLVYT TGCGVHAFTY 190 200 210 220 230 240 DPSLGVFCLC QERMRFPEKG KTYSINEGNY IKFPNGVKKY IKFCQEEDKS TNRPYTSRYI 250 260 270 280 290 300 GSLVADFHRN LLKGGIYLYP STASHPDGKL RLLYECNPMA FLAEQAGGKA SDGKERILDI 310 320 330 IPETLHQRRS FFVGNDHMVE DVERFIREFP DA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the Escherichia coli fructose-1,6-bisphosphatase gene." Hamilton W.D.O., Harrison D.A., Dyer T.A. Nucleic Acids Res. 16:8707-8707(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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]	"Amino acid sequence homology among fructose-1,6-bisphosphatases." Marcus F., Gontero B., Harrsch P.B., Rittenhouse J. Biochem. Biophys. Res. Commun. 135:374-381(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 43-62; 220-229; 239-249; 254-269 AND 297-308.
[6]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[7]	"Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase." Hines J.K., Fromm H.J., Honzatko R.B. J. Biol. Chem. 281:18386-18393(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SULFATE IONS, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[8]	"Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state." Hines J.K., Fromm H.J., Honzatko R.B. J. Biol. Chem. 282:11696-11704(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEXES WITH FRUCTOSE-6-PHOSPHATE; CITRATE AND PHOSPHOENOLPYRUVATE, ENZYME REGULATION, SUBUNIT.
[9]	"Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch." Hines J.K., Kruesel C.E., Fromm H.J., Honzatko R.B. J. Biol. Chem. 282:24697-24706(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-1,6-BIPHOSPHATE; MAGNESIUM IONS; AMP AND GLUCOSE-6-PHOSPHATE, SUBUNIT, COFACTOR, ENZYME REGULATION.
[10]	"Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition." Hines J.K., Chen X., Nix J.C., Fromm H.J., Honzatko R.B. J. Biol. Chem. 282:36121-36131(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BIPHOSPHATE; MAGNESIUM IONS AND CITRATE, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12545 mRNA. Translation: CAA31062.1.
U14003 Genomic DNA. Translation: AAA97129.1.
U00096 Genomic DNA. Translation: AAC77189.1.
AP009048 Genomic DNA. Translation: BAE78232.1.

PIR

PAEC. S01383.

RefSeq

NP_418653.1. NC_000913.2.
YP_492373.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GQ1	X-ray	1.45	A	1-332	[»]
2OWZ	X-ray	2.18	A	1-332	[»]
2OX3	X-ray	2.18	A	1-332	[»]
2Q8M	X-ray	2.05	A/B	1-332	[»]
2QVR	X-ray	2.18	A	1-332	[»]

ProteinModelPortal

P0A993.

SMR

P0A993. Positions 1-332.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b4232.

2D gel databases

SWISS-2DPAGE

P0A993.

Proteomic databases

PaxDb

P0A993.

PRIDE

P0A993.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77189; AAC77189; b4232.
BAE78232; BAE78232; BAE78232.

GeneID

12930322.
948753.

KEGG

ecj:Y75_p4117.
eco:b4232.

PATRIC

32124037. VBIEscCol129921_4363.

Organism-specific databases

EchoBASE

EB0279.

EcoGene

EG10283. fbp.

Phylogenomic databases

eggNOG

COG0158.

HOGENOM

HOG000191265.

KO

K03841.

OMA

CQEEDKA.

ProtClustDB

PRK09293.

Enzyme and pathway databases

BioCyc

EcoCyc:F16B-MONOMER.
ECOL316407:JW4191-MONOMER.
MetaCyc:F16B-MONOMER.

SABIO-RK

P0A993.

UniPathway

UPA00138.

Gene expression databases

Genevestigator

P0A993.

Family and domain databases

HAMAP

MF_01855. FBPase_class1.

InterPro

IPR000146. FBPase_class-1/SBPase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]

PANTHER

PTHR11556. PTHR11556. 1 hit.

Pfam

PF00316. FBPase. 1 hit.
[Graphical view]

PIRSF

PIRSF000904. FBPtase_SBPase. 1 hit.

PRINTS

PR00115. F16BPHPHTASE.

PROSITE

PS00124. FBPASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A993.

Entry information

Entry name

F16PA_ECOLI

Accession

Primary (citable) accession number: P0A993
Secondary accession number(s): P09200, Q2M674

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program