Fructose-1,6-bisphosphatase 1 - Ovis aries (Sheep)

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P09199 (F16P1_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Ovis aries (Sheep)

Taxonomic identifier

9940 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis

Protein attributes

Sequence length	337 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 Phosphoprotein
Technical term	Allosteric enzyme Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular response to drug Inferred from sequence or structural similarity. Source: UniProtKB cellular response to magnesium ion Inferred from sequence or structural similarity. Source: UniProtKB fructose 6-phosphate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB gluconeogenesis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of Ras protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of glycolysis Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB regulation of gluconeogenesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB soluble fraction Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	AMP binding Inferred from sequence or structural similarity. Source: UniProtKB fructose 1,6-bisphosphate 1-phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from sequence or structural similarity. Source: UniProtKB monosaccharide binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.1 Ref.2

Chain

2 – 337

336

Fructose-1,6-bisphosphatase 1

PRO_0000200503

Regions

Nucleotide binding

18 – 22

AMP By similarity

Nucleotide binding

28 – 32

AMP By similarity

Nucleotide binding

113 – 114

AMP By similarity

Region

122 – 125

Substrate binding By similarity

Region

213 – 216

Substrate binding By similarity

Region

244 – 249

Substrate binding By similarity

Region

275 – 277

Substrate binding By similarity

Sites

Metal binding

Magnesium 1 By similarity

Metal binding

Magnesium 1 By similarity

Metal binding

Magnesium 2 By similarity

Metal binding

119

Magnesium 2 By similarity

Metal binding

119

Magnesium 3 By similarity

Metal binding

121

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

122

Magnesium 3 By similarity

Metal binding

281

Magnesium 3 By similarity

Binding site

141

AMP By similarity

Binding site

265

Substrate By similarity

Amino acid modifications

Modified residue

N-acetylthreonine Ref.1 Ref.2

Modified residue

208

Phosphoserine; by PKA Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P09199 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4477539DA1AF9334
Show »

FASTA

337

36,675

        10         20         30         40         50         60 
MTDEAPFDTN IVTVTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI 

        70         80         90        100        110        120 
AGTTNVTGDQ VKKLDVLSND LVVNVLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP 

       130        140        150        160        170        180 
LDGSSNIDCL VSIGTIFGIY KKISKDDPSE KDALQPGRNL VAAGYALYGS ATMLVLAMVN 

       190        200        210        220        230        240 
GVNCFMLDPA IGEFILVDRD VKIKKKGSIY SLNEGYAKDF DPALTEYVQR KKFPPDNSAP 

       250        260        270        280        290        300 
YGSRYVGSMV ADVHRTLVYG GIFMYPADKK SPSGKLRLLY ECDPMAYVIE KAGGMATTGK 

       310        320        330 
EAVLDIVPTD IHQKVPIILG SPEDVTEFLE IKKYTAK

« Hide

References

[1]	"Amino acid sequence studies on sheep liver fructose-bisphosphatase. II. The complete sequence." Fisher W.K., Thompson E.O.P. Aust. J. Biol. Sci. 36:235-250(1983) [PubMed: 6316885] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-337, ACETYLATION AT THR-2, PHOSPHORYLATION AT SER-208.
[2]	"Amino acid sequence studies on sheep liver fructose-bisphosphatase. I. The S-peptide." Fisher W.K., Thompson E.O.P. Aust. J. Biol. Sci. 33:665-674(1980) [PubMed: 6264908] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-61, ACETYLATION AT THR-2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	A05318.
3D structure databases
ProteinModelPortal	P09199.
SMR	P09199. Positions 2-337.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG005627.
Family and domain databases
InterPro	IPR000146. FBPase_class-1/SBPase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
PANTHER	PTHR11556. In_FB_phphtase. 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...

Entry information

Entry name

F16P1_SHEEP

Accession

Primary (citable) accession number: P09199

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents