Reviewed, UniProtKB/Swiss-Prot P19112 (F16P1_RAT)

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	363 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. Ref.6
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 insulin stimulus Ref.1 Inferred from expression pattern. Source: RGD fructose 6-phosphate metabolic process Inferred from direct assay. Source: RGD gluconeogenesis Inferred from direct assay. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	fructose 1,6-bisphosphate 1-phosphatase activity Inferred from direct assay. Source: RGD magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW monosaccharide binding Inferred from direct assay. Source: RGD
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 – 363	362	Fructose-1,6-bisphosphatase 1		PRO_0000200502
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 By similarity
	Metal binding	119	1	Magnesium 2 By similarity
	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-acetylvaline Ref.8
	Modified residue	353	1	Phosphoserine Ref.7
Experimental info
	Mutagenesis	275	1	K → A: Reduces affinity for substrate 20-fold, and decreases affinity for the competitive inhibitor fructose-2,6-biphosphate 500-fold. Ref.6
	Sequence conflict	148	1	P → A in AAA41131. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P19112-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0470F1A2EA917D6F	FASTA	363	39,609
	10 20 30 40 50 60 MVDHAPFETD ISTLTRFVLE EGRKAGGTGE MTQLLNSLCT AIKAISSAVR QAGIAQLYGI 70 80 90 100 110 120 AGSTNVTGDQ VKKLDILSND LVINMLKSSY ATCVLVSEED THAIIIEPEK RGKYVVCFDP 130 140 150 160 170 180 LDGSSNIDCL ASIGTIFGIY RKTSANEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMNC 190 200 210 220 230 240 GVNCFMLDPS IGEFILVDRD VKIKKKGNIY SINEGYAKDF DPAINEYIQR KKFPPDNSAP 250 260 270 280 290 300 YGARYVGSMV ADVHRTLVYG GIFLYPANKK NPSGKLRLLY ECNPIAYVME KAGGLATTGN 310 320 330 340 350 360 EDILDIVPTE IHQKAPVIMG STEDVQEFLE IYNKDKAKSR PSLPLPQSRA RESPVHSICD ELF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence of rat liver fructose-1,6-bisphosphatase and evidence for down-regulation of its mRNA by insulin." El-Maghrabi M.R., Pilkis J., Marker A.J., Colosia A.D., D'Angelo G., Fraser B.A., Pilkis S.J. Proc. Natl. Acad. Sci. U.S.A. 85:8430-8434(1988) [PubMed: 2847161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"The rat fructose-1,6-bisphosphatase gene. Structure and regulation of expression." El-Maghrabi M.R., Lange A.J., Kummel L., Pilkis S.J. J. Biol. Chem. 266:2115-2120(1991) [PubMed: 1846613] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley.
[3]	"Liver fructose-1,6-bisphosphatase cDNA: trans-complementation of fission yeast and characterization of two human transcripts." Bertolotti R., Armbruster-Hilbert L., Okayama H. Differentiation 59:51-60(1995) [PubMed: 7589895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"Amino acid sequence of the COOH-terminal region of fructose-1,6-bisphosphatases in relation to cyclic AMP-dependent phosphorylation." Rittenhouse J., Chatterjee T., Marcus F., Reardon I., Heinrikson R.L. J. Biol. Chem. 258:7648-7652(1983) [PubMed: 6305949] [Abstract] Cited for: PROTEIN SEQUENCE OF 320-362. Tissue: Liver.
[6]	"Lysine 274 is essential for fructose 2,6-bisphosphate inhibition of fructose-1,6-bisphosphatase." el-Maghrabi M.R., Austin L.R., Correia J.J., Pilkis S.J. J. Biol. Chem. 267:6526-6530(1992) [PubMed: 1313010] [Abstract] Cited for: MUTAGENESIS OF LYS-275, ENZYME REGULATION.
[7]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed: 16396499] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Identification of novel protein targets regulated by maternal dietary fatty acid composition in neonatal rat liver." Novak E.M., Lee E.K., Innis S.M., Keller B.O. J. Proteomics 73:41-49(2009) [PubMed: 19651254] [Abstract] Cited for: ACETYLATION AT VAL-2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04112 mRNA. Translation: AAA60739.1. M57284 , M57274, M57279, M57278, M57282, M57281 Genomic DNA. Translation: AAA41131.1. M86240 mRNA. Translation: AAA86425.1. BC078894 mRNA. Translation: AAH78894.1. BC078895 mRNA. Translation: AAH78895.1.
IPI	IPI00231745.
PIR	A31342.
RefSeq	NP_036690.2.
UniGene	Rn.33703
3D structure databases
SMR	P19112. Positions 7-338.
ModBase	Search...
PTM databases
PhosphoSite	P19112.
Proteomic databases
PRIDE	P19112.
Genome annotation databases
Ensembl	ENSRNOT00000023685; ENSRNOP00000023685; ENSRNOG00000017597; Rattus norvegicus. [Genome view]
GeneID	24362.
KEGG	rno:24362.
UCSC	NM_012558. rat.
Organism-specific databases
CTD	24362.
RGD	2595. Fbp1.
Phylogenomic databases
eggNOG	maNOG08767.
HOVERGEN	P19112.
PhylomeDB	P19112.
Enzyme and pathway databases
BRENDA	3.1.3.11. 248.
Gene expression databases
Genevestigator	P19112.
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...
Other Resources
NextBio	603091.

Entry information

Entry name

F16P1_RAT

Accession

Primary (citable) accession number: P19112
Secondary accession number(s): Q64594

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)