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	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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

Chain

1 – 337

337

Fructose-1,6-bisphosphatase 1

PRO_0000200501

Regions

Nucleotide binding

17 – 21

5

AMP By similarity

Nucleotide binding

27 – 31

5

AMP By similarity

Nucleotide binding

112 – 113

2

AMP By similarity

Region

121 – 124

4

Substrate binding By similarity

Region

212 – 215

4

Substrate binding By similarity

Region

243 – 248

6

Substrate binding By similarity

Region

274 – 276

3

Substrate binding By similarity

Sites

Metal binding

68

1

Magnesium 1 By similarity

Metal binding

97

1

Magnesium 1 By similarity

Metal binding

97

1

Magnesium 2

Metal binding

118

1

Magnesium 2

Metal binding

118

1

Magnesium 3 By similarity

Metal binding

120

1

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

121

1

Magnesium 3 By similarity

Metal binding

280

1

Magnesium 3 By similarity

Binding site

140

1

AMP By similarity

Binding site

264

1

Substrate By similarity

Amino acid modifications

Modified residue

1

1

N-acetylalanine Ref.1

Experimental info

Sequence conflict

83

1

N → D AA sequence Ref.5

Sequence conflict

88

1

S → A AA sequence Ref.5

Sequence conflict

92

1

C → S AA sequence Ref.5

Sequence conflict

115 – 116

2

VC → SN AA sequence Ref.5

Sequence conflict

121 – 122

2

DG → VP AA sequence Ref.5

Sequence conflict

267

1

N → D AA sequence Ref.6

Sequence conflict

280

1

E → Q AA sequence Ref.6

Sequence conflict

283

1

Missing AA sequence Ref.6

Sequence conflict

300

1

E → Q AA sequence Ref.6

Sequence conflict

307 – 312

6

PTDIHQ → QTPDH AA sequence Ref.6

Sequence conflict

326

1

E → Q AA sequence Ref.6

Sequence conflict

329 – 330

2

Missing AA sequence Ref.6

Secondary structure

1

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337

Helix Strand Turn

Details...

Helix

13 – 24

12

Helix

29 – 48

20

Turn

49 – 52

4

Helix

73 – 87

15

Beta strand

91 – 96

6

Helix

107 – 109

3

Beta strand

110 – 121

12

Helix

125 – 128

4

Beta strand

132 – 140

9

Helix

149 – 152

4

Helix

156 – 158

3

Beta strand

160 – 177

18

Beta strand

180 – 187

8

Turn

188 – 191

4

Beta strand

192 – 197

6

Beta strand

207 – 210

4

Helix

213 – 218

6

Helix

221 – 231

11

Helix

248 – 258

11

Beta strand

261 – 264

4

Beta strand

274 – 276

3

Turn

277 – 280

4

Helix

281 – 291

11

Beta strand

294 – 296

3

Beta strand

298 – 301

4

Helix

302 – 304

3

Beta strand

316 – 319

4

Helix

321 – 332

12

Turn

333 – 335

3

Sequences

	Sequence		Length	Mass (Da)
	P00637-1 [UniParc]. Last modified December 15, 1998. Version 3. Checksum: 72FC502C43B75151	FASTA	337	36,447
	10 20 30 40 50 60 ADKAPFDTDI STMTRFVMEE GRKAGGTGEM TQLLNSLCTA VKAISTAVRK AGIAHLYGIA 70 80 90 100 110 120 GSTNVTGDQV KKLDVLSNDL VMNMLKSSFA TCVLVSEEDK NAIIVEPEKR GKYVVCFDPL 130 140 150 160 170 180 DGSSNIDCLV SIGTIFGIYR KKSTDEPSTK DALQPGRNLV AAGYALYGSA TMLVLAGGSG 190 200 210 220 230 240 VNSFMLDPAI GEFILVDKNV KIKKKGNIYS LNEGYAKDFD PAVTEYIQKK KFPPDNSSPY 250 260 270 280 290 300 GARYVGSMVA DVHRTLVYGG IFLYPANKKS PDGKLRLLYE CNPMAFIMEK AGGMATTGKE 310 320 330 AILDIVPTDI HQRAPVILGS PDDVQEFLEI YKKHAVK

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. 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 1-18. 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 16-60. 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 19-77. 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 83-122 AND 135-154, 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 248-288 AND 295-337, 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

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BK4	X-ray	2.30	A	1-337	[»]

ModBase

Search...

Phylogenomic databases

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.

ProDom

PD001491. In_FB_phphtase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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:	December 15, 1998
Last modified:	September 22, 2009
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)