Reviewed, UniProtKB/Swiss-Prot P00637 (F16P1_RABIT)

Names and origin

Protein names

Recommended name:
    Fructose-1,6-bisphosphatase 1
      Short name=FBPase 1
    EC=3.1.3.11
Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 1

Gene names

Name:	FBP1
Synonyms:	FBP

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
Enzyme regulation	Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose-2,6-biphosphate acts as competitive inhibitor. Fructose-2,6-biphosphate and AMP have synergistic effects By similarity.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the FBPase class 1 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Gluconeogenesis
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological process	gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: EC magnesium ion 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

Initiator methionine

1

1

Removed Ref.1 Ref.2

Chain

2 – 338

337

Fructose-1,6-bisphosphatase 1

PRO_0000200501

Regions

Nucleotide binding

18 – 22

5

AMP By similarity

Nucleotide binding

28 – 32

5

AMP By similarity

Nucleotide binding

113 – 114

2

AMP By similarity

Region

122 – 125

4

Substrate binding By similarity

Region

213 – 216

4

Substrate binding By similarity

Region

244 – 249

6

Substrate binding By similarity

Region

275 – 277

3

Substrate binding By similarity

Sites

Metal binding

69

1

Magnesium 1 By similarity

Metal binding

98

1

Magnesium 1 By similarity

Metal binding

98

1

Magnesium 2

Metal binding

119

1

Magnesium 2

Metal binding

119

1

Magnesium 3 By similarity

Metal binding

121

1

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

122

1

Magnesium 3 By similarity

Metal binding

281

1

Magnesium 3 By similarity

Binding site

141

1

AMP By similarity

Binding site

265

1

Substrate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine

Experimental info

Sequence conflict

84

1

N → D AA sequence Ref.5

Sequence conflict

89

1

S → A AA sequence Ref.5

Sequence conflict

93

1

C → S AA sequence Ref.5

Sequence conflict

116 – 117

2

VC → SN AA sequence Ref.5

Sequence conflict

122 – 123

2

DG → VP AA sequence Ref.5

Sequence conflict

268

1

N → D AA sequence Ref.6

Sequence conflict

281

1

E → Q AA sequence Ref.6

Sequence conflict

284

1

Missing AA sequence Ref.6

Sequence conflict

301

1

E → Q AA sequence Ref.6

Sequence conflict

308 – 313

6

PTDIHQ → QTPDH AA sequence Ref.6

Sequence conflict

327

1

E → Q AA sequence Ref.6

Sequence conflict

330 – 331

2

Missing AA sequence Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

338

Helix Strand Turn

Details...

Helix

14 – 25

12

Helix

30 – 49

20

Turn

50 – 53

4

Helix

74 – 88

15

Beta strand

92 – 97

6

Helix

108 – 110

3

Beta strand

111 – 122

12

Helix

126 – 129

4

Beta strand

133 – 141

9

Helix

150 – 153

4

Helix

157 – 159

3

Beta strand

161 – 178

18

Beta strand

181 – 188

8

Turn

189 – 192

4

Beta strand

193 – 198

6

Beta strand

208 – 211

4

Helix

214 – 219

6

Helix

222 – 232

11

Helix

249 – 259

11

Beta strand

262 – 265

4

Beta strand

275 – 277

3

Turn

278 – 281

4

Helix

282 – 292

11

Beta strand

295 – 297

3

Beta strand

299 – 302

4

Helix

303 – 305

3

Beta strand

317 – 320

4

Helix

322 – 333

12

Turn

334 – 336

3

Sequences

	Sequence		Length	Mass (Da)
	P00637-1 [UniParc]. Last modified November 24, 2009. Version 4. Checksum: 2676BF5964461250	FASTA	338	36,578
	10 20 30 40 50 60 MADKAPFDTD ISTMTRFVME EGRKAGGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI 70 80 90 100 110 120 AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KNAIIVEPEK RGKYVVCFDP 130 140 150 160 170 180 LDGSSNIDCL VSIGTIFGIY RKKSTDEPST KDALQPGRNL VAAGYALYGS ATMLVLAGGS 190 200 210 220 230 240 GVNSFMLDPA IGEFILVDKN VKIKKKGNIY SLNEGYAKDF DPAVTEYIQK KKFPPDNSSP 250 260 270 280 290 300 YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPDGKLRLLY ECNPMAFIME KAGGMATTGK 310 320 330 EAILDIVPTD IHQRAPVILG SPDDVQEFLE IYKKHAVK

References

[1]	"Fructose-1,6-bisphosphatase. Primary structure of the rabbit liver enzyme. 'Intermediate' variability of an oligomeric protein." Kaiser R., Olsson H., Erman M., Weeks C.M., Hjelmqvist L., Ghosh D., Joernvall H. FEBS Lett. 389:249-252(1996) [PubMed: 8766709] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-338. Tissue: Liver.
[2]	"Rabbit liver fructose 1,6-bisphosphatase: the sequence of the amino-terminal region." El-Dorry H.A., Chu D.K., Dzugaj A., Tsolas O., Pontremoli S., Horecker B.L. Arch. Biochem. Biophys. 178:200-207(1977) [PubMed: 189691] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-19. Strain: New Zealand white. Tissue: Liver.
[3]	"Primary structure of the S-peptide formed by digestion of rabbit liver fructose 1,6-biphosphatase with subtilisin." El-Dorry H.A., Chu D.K., Dzugaj A., Botelho L.H., Pontremoli S., Horecker B.L. Arch. Biochem. Biophys. 182:763-773(1977) [PubMed: 197893] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-61. Strain: New Zealand white. Tissue: Liver.
[4]	"Digestion of rabbit liver fructose 1,6-bisphosphatase with subtilisin: sites of cleavage and activity of the modified enzyme." Botelho L.H., El-Dorry H.A., Crivellaro O., Chu D.K., Pontremoli S., Horecker B.L. Arch. Biochem. Biophys. 184:535-545(1977) [PubMed: 202200] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-78. Strain: New Zealand white. Tissue: Liver.
[5]	"Location of lysyl residues at the allosteric site of fructose 1,6-bisphosphatase." Suda H., Xu G.-J., Kutny R.M., Natalini P., Pontremoli S., Horecker B.L. Arch. Biochem. Biophys. 217:10-14(1982) [PubMed: 6289748] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 84-123 AND 136-155, ALLOSTERIC REGULATION. Tissue: Liver.
[6]	"Rabbit liver fructose-1,6-bisphosphatase: location of an active site lysyl residue in the COOH-terminal fragment generated by a lysosomal proteinase." Xu G.J., Natalini P., Suda H., Tsolas O., Dzugaj A., Sun S.C., Pontremoli S., Horecker B.L. Arch. Biochem. Biophys. 214:688-694(1982) [PubMed: 6284034] [Abstract] Cited for: PROTEIN SEQUENCE OF 249-289 AND 296-338, ACTIVE SITE. Tissue: Liver.
[7]	"Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution." Weeks C.M., Roszak A.W., Erman M., Kaiser R., Joernvall H., Ghosh D. Acta Crystallogr. D 55:93-102(1999) [PubMed: 10089399] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.

Cross-references

Sequence databases

PIR

S70469.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BK4	X-ray	2.30	A	2-338	[»]

ModBase

Search...

Phylogenomic databases

eggNOG

maNOG08767.

HOVERGEN

P00637.

Enzyme and pathway databases

BRENDA

3.1.3.11. 255.

Family and domain databases

InterPro

IPR000146. Fructose_bisphosphatase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]

PANTHER

PTHR11556. In_FB_phphtase. 1 hit.

Pfam

PF00316. FBPase. 1 hit.
[Graphical view]

PRINTS

PR00115. F16BPHPHTASE.

PROSITE

PS00124. FBPASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

F16P1_RABIT

Accession

Primary (citable) accession number: P00637

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 24, 2009
Last modified:	February 9, 2010
This is version 82 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)