Q9QXD6 (F16P1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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 transcript 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	Allosteric enzyme Complete proteome Reference proteome
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	1	1	Removed By similarity
	Chain	2 – 338	337	Fructose-1,6-bisphosphatase 1		PRO_0000200499
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-acetylalanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9QXD6 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 50AE999F0D517E4F	FASTA	338	36,912
	10 20 30 40 50 60 MANHAPFETD ISTLTRFVME QGRKAQGTGE LTQLLNSLCT AIKAISSAVR QAGIAQLYGI 70 80 90 100 110 120 AGSTNVTGDQ VKKLDILSND LVINMLKSSY ATCVLVSEEN TNAIIIEPEK RGKYVVCFDP 130 140 150 160 170 180 LDGSSNIDCL VSIGTIFGIY RKKSTDEPSE KDALQPGRDL VAAGYALYGS ATMLVLAMDC 190 200 210 220 230 240 GVNCFMLDPS IGEFIMVDRD VKMKKKGNIY SLNEGYAKDF DPAINEYLQR KKFPPDGSAP 250 260 270 280 290 300 YGARYVGSMV ADIHRTLVYG GIFLYPANKK SPSGKLRLLY ECNPIAYVME KAGGLATTGD 310 320 330 KDILDIVPTE IHQKAPVVMG SSEDVQEFLE IYRKHKAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the mouse liver fructose-1,6-bisphosphatase gene." Stein S., Liehr T., Eschrich K. Gene 264:215-224(2001) [PubMed: 11250076] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney and Liver.
[3]	"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]. Strain: FVB/N. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ132693 mRNA. Translation: CAB65244.1. AK002216 mRNA. Translation: BAB21941.1. AK149527 mRNA. Translation: BAE28940.1. BC011480 mRNA. Translation: AAH11480.1. BC051392 mRNA. Translation: AAH51392.1.
IPI	IPI00228630.
RefSeq	NP_062268.1. NM_019395.2.
UniGene	Mm.423078.
3D structure databases
ProteinModelPortal	Q9QXD6.
SMR	Q9QXD6. Positions 13-335.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QXD6. 1 interaction.
STRING	Q9QXD6.
PTM databases
PhosphoSite	Q9QXD6.
2D gel databases
REPRODUCTION-2DPAGE	IPI00228630. Q9QXD6.
Proteomic databases
PRIDE	Q9QXD6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000092888; ENSMUSP00000090564; ENSMUSG00000069805.
GeneID	14121.
KEGG	mmu:14121.
NMPDR	fig|10090.3.peg.28005.
UCSC	uc007qxg.1. mouse.
Organism-specific databases
CTD	2203.
MGI	MGI:95492. Fbp1.
Phylogenomic databases
eggNOG	roNOG08567.
GeneTree	ENSGT00390000015513.
HOGENOM	HBG731261.
HOVERGEN	HBG005627.
InParanoid	Q9QXD6.
OMA	YGSATMV.
OrthoDB	EOG4P8FJF.
PhylomeDB	Q9QXD6.
Gene expression databases
ArrayExpress	Q9QXD6.
Bgee	Q9QXD6.
CleanEx	MM_FBP1.
Genevestigator	Q9QXD6.
GermOnline	ENSMUSG00000069805. Mus musculus.
Family and domain databases
InterPro	IPR000146. FBPase_class-1/SBPase. IPR020548. Fructose_bisphosphatase_AS. [Graphical view]
KO	K03841.
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...
Other
NextBio	285192.
SOURCE	Search...

Entry information

Entry name

F16P1_MOUSE

Accession

Primary (citable) accession number: Q9QXD6
Secondary accession number(s): Q3UEH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program