Reviewed, UniProtKB/Swiss-Prot P00636 (F16P1_PIG)

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

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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 + H(2)O = D-fructose 6-phosphate + phosphate.
Enzyme regulation	Inhibited by AMP, which affects the turnover of bound substrate and not the affinity for substrate.
Pathway	Carbohydrate biosynthesis; gluconeogenesis.
Subunit structure	Homotetramer. With four binding sites each for the substrate, for AMP, and for divalent metal cation (the greatest affinity is for zinc).
Miscellaneous	The molecule has a highly reactive cysteine residue (Cys-117 or Cys-129), which tends to form mixed disulfides (e.g., with homocystine) but is not essential for enzyme activity.
Sequence similarities	Belongs to the FBPase class 1 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Gluconeogenesis
Ligand	Zinc
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
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 zinc 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

Chain

2 – 338

337

Fructose-1,6-bisphosphatase 1

PRO_0000200500

Sites

Active site

275

1

Binding site

142

1

Allosteric inhibitor

Amino acid modifications

Modified residue

2

1

N-acetylthreonine

Modified residue

208

1

Phosphoserine; by PKA

Experimental info

Sequence conflict

2

1

T → A AA sequence Ref.3

Sequence conflict

4

1

Q → E AA sequence Ref.3

Sequence conflict

21

1

E → Q AA sequence Ref.2

Sequence conflict

97

1

S → T AA sequence Ref.2

Sequence conflict

157

1

G → E AA sequence Ref.2

Sequence conflict

200

1

D → N AA sequence Ref.2

Sequence conflict

229

1

Q → E AA sequence Ref.2

Secondary structure

1

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338

Helix Strand Turn

Details...

Helix

14 – 24

11

Helix

30 – 50

21

Turn

51 – 56

6

Beta strand

59 – 64

6

Beta strand

70 – 72

3

Helix

73 – 88

16

Beta strand

92 – 97

6

Helix

108 – 110

3

Beta strand

111 – 122

12

Helix

124 – 126

3

Turn

127 – 130

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 – 291

10

Beta strand

295 – 297

3

Beta strand

299 – 302

4

Helix

303 – 305

3

Beta strand

317 – 320

4

Helix

322 – 334

13

Sequences

	Sequence		Length	Mass (Da)
	P00636-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 610BF8D3C6D320F6	FASTA	338	36,779
	10 20 30 40 50 60 MTDQAAFDTN IVTLTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI 70 80 90 100 110 120 AGSTNVTGDQ VKKLDVLSND LVINVLKSSF ATCVLVSEED KNAIIVEPEK RGKYVVCFDP 130 140 150 160 170 180 LDGSSNIDCL VSIGTIFGIY RKNSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMVN 190 200 210 220 230 240 GVNCFMLDPA IGEFILVDRD VKIKKKGSIY SINEGYAKEF DPAITEYIQR KKFPPDNSAP 250 260 270 280 290 300 YGARYVGSMV ADVHRTLVYG GIFMYPANKK SPKGKLRLLY ECNPMAYVME KAGGLATTGK 310 320 330 EAVLDIVPTD IHQRAPIILG SPEDVTELLE IYQKHAAK

References

[1]	"Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase." Williams M.K., Kantrowitz E.R. Proc. Natl. Acad. Sci. U.S.A. 89:3080-3082(1992) [PubMed: 1313579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase." Marcus F., Edelstein I., Reardon I., Heinrikson R.L. Proc. Natl. Acad. Sci. U.S.A. 79:7161-7165(1982) [PubMed: 6296821] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-336. Tissue: Kidney cortex.
[3]	"Conservation of primary structure at the proteinase-sensitive site of fructose 1,6-bisphosphatases." McGregor J.S., Hannappel E., Xu G.-J., Pontremoli S., Horecker B.L. Arch. Biochem. Biophys. 217:652-664(1982) [PubMed: 6291465] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24 AND 44-61. Tissue: Kidney.
[4]	"Mechanism of action of fructose 1,6-bisphosphatase." Benkovic S.J., Demaine M.M. Adv. Enzymol. Relat. Areas Mol. Biol. 53:45-82(1982) [PubMed: 6277165] [Abstract] Cited for: SUBSTRATE-BINDING SITE, LIGANDS, REVIEW.
[5]	"Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8-A resolution." Ke H.M., Thorpe C.M., Seaton B.A., Lipscomb W.N., Marcus F. J. Mol. Biol. 212:513-539(1990) [PubMed: 2157849] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SEQUENCE REVISION.
[6]	"Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium." Ke H.M., Zhang Y.P., Lipscomb W.N. Proc. Natl. Acad. Sci. U.S.A. 87:5243-5247(1990) [PubMed: 2164670] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[7]	"Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution." Ke H.M., Zhang Y.P., Liang J.-Y., Lipscomb W.N. Proc. Natl. Acad. Sci. U.S.A. 88:2989-2993(1991) [PubMed: 1849642] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[8]	"Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution." Liang J.-Y., Huang S., Zhang Y.P., Ke H.M., Lipscomb W.N. Proc. Natl. Acad. Sci. U.S.A. 89:2404-2408(1992) [PubMed: 1312721] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[9]	"Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase." Choe J.Y., Poland B.W., Fromm H.J., Honzatko R.B. Biochemistry 37:11441-11450(1998) [PubMed: 9708979] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
[10]	"Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes." Choe J.Y., Fromm H.J., Honzatko R.B. Biochemistry 39:8565-8574(2000) [PubMed: 10913263] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M86347 mRNA. Translation: AAA31035.1.

PIR

PAPGF. S37696.

RefSeq

NP_999144.1.

UniGene

Ssc.5127

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CNQ	X-ray	2.27	A	1-338	[»]
1EYI	X-ray	2.32	A	1-338	[»]
1EYJ	X-ray	2.28	A/B	1-338	[»]
1EYK	X-ray	2.23	A/B	1-338	[»]
1FBC	X-ray	2.60	A/B	1-336	[»]
1FBD	X-ray	2.90	A/B	1-336	[»]
1FBE	X-ray	3.00	A/B	1-336	[»]
1FBF	X-ray	2.70	A/B	1-336	[»]
1FBG	X-ray	3.00	A/B	1-336	[»]
1FBH	X-ray	2.50	A/B	1-336	[»]
1FBP	X-ray	2.50	A/B	1-336	[»]
1FJ6	X-ray	2.50	A	1-338	[»]
1FJ9	X-ray	2.50	A/B	1-338	[»]
1FPB	X-ray	2.60	A/B	1-336	[»]
1FPD	X-ray	2.10	A/B	1-336	[»]
1FPE	X-ray	2.20	A/B	1-336	[»]
1FPF	X-ray	2.10	A/B	1-336	[»]
1FPG	X-ray	2.30	A/B	1-336	[»]
1FPI	X-ray	2.30	A/B	1-336	[»]
1FPJ	X-ray	2.20	A/B	1-336	[»]
1FPK	X-ray	3.00	A/B	1-336	[»]
1FPL	X-ray	2.30	A/B	1-336	[»]
1FRP	X-ray	2.00	A/B	1-336	[»]
1FSA	X-ray	2.30	A/B	1-338	[»]
1KZ8	X-ray	2.00	A/F	1-338	[»]
1LEV	X-ray	2.15	A/F	1-338	[»]
1NUW	X-ray	1.30	A	1-338	[»]
1NUX	X-ray	1.60	A	1-338	[»]
1NUY	X-ray	1.30	A	1-338	[»]
1NUZ	X-ray	1.90	A	1-338	[»]
1NV0	X-ray	1.80	A	1-338	[»]
1NV1	X-ray	1.90	A	1-338	[»]
1NV2	X-ray	2.10	A	1-338	[»]
1NV3	X-ray	2.00	A	1-338	[»]
1NV4	X-ray	1.90	A	1-338	[»]
1NV5	X-ray	1.90	A	1-338	[»]
1NV6	X-ray	2.15	A	1-338	[»]
1NV7	X-ray	2.15	A/B	1-338	[»]
1Q9D	X-ray	2.35	A/B	1-338	[»]
1RDX	X-ray	2.75	A/B	1-338	[»]
1RDY	X-ray	2.20	A/B	1-338	[»]
1RDZ	X-ray	2.05	A/B	1-338	[»]
1YXI	X-ray	2.00	A	1-338	[»]
1YYZ	X-ray	1.85	A	1-338	[»]
1YZ0	X-ray	2.07	A/B	1-338	[»]
2F3B	X-ray	1.80	A	1-338	[»]
2F3D	X-ray	1.83	A	1-338	[»]
2F3H	X-ray	2.70	A/B	1-338	[»]
2FBP	X-ray	2.80	A/B	1-336	[»]
2QVU	X-ray	1.50	A/B	2-338	[»]
2QVV	X-ray	2.03	A/B	2-338	[»]
3FBP	X-ray	2.80	A/B	1-336	[»]
4FBP	X-ray	2.50	A/B/C/D	1-336	[»]
5FBP	X-ray	2.10	A/B	1-336	[»]

ModBase

Search...

Genome annotation databases

GeneID

397038.

KEGG

ssc:397038.

Phylogenomic databases

HOVERGEN

P00636.

Family and domain databases

InterPro

IPR000146. In_FB_phphtase.
[Graphical view]

PANTHER

PTHR11556. In_FB_phphtase. 1 hit.

Pfam

PF00316. FBPase. 1 hit.
[Graphical view]

PRINTS

PR00115. FBPHPHTASE.
PR00377. INFBPHPHTASE.

ProDom

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

PROSITE

PS00124. FBPASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources