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Reviewed, UniProtKB/Swiss-Prot Q9QXD6 (F16P1_MOUSE)

Last modified January 19, 2010. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCarbohydrate metabolism
Gluconeogenesis
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionfructose 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 338337Fructose-1,6-bisphosphatase 1
PRO_0000200499

Regions

Nucleotide binding18 – 225AMP By similarity
Nucleotide binding28 – 325AMP By similarity
Nucleotide binding113 – 1142AMP By similarity
Region122 – 1254Substrate binding By similarity
Region213 – 2164Substrate binding By similarity
Region244 – 2496Substrate binding By similarity
Region275 – 2773Substrate binding By similarity

Sites

Metal binding691Magnesium 1 By similarity
Metal binding981Magnesium 1 By similarity
Metal binding981Magnesium 2 By similarity
Metal binding1191Magnesium 2 By similarity
Metal binding1191Magnesium 3 By similarity
Metal binding1211Magnesium 2; via carbonyl oxygen By similarity
Metal binding1221Magnesium 3 By similarity
Metal binding2811Magnesium 3 By similarity
Binding site1411AMP By similarity
Binding site2651Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9QXD6-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 50AE999F0D517E4F

FASTA33836,912
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
IPIIPI00228630.
RefSeqNP_062268.1.
UniGeneMm.423078

3D structure databases

SMRQ9QXD6. Positions 7-338.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9QXD6.

PTM databases

PhosphoSiteQ9QXD6.

2-D gel databases

REPRODUCTION-2DPAGEQ9QXD6.

Proteomic databases

PRIDEQ9QXD6.

Genome annotation databases

EnsemblENSMUST00000092888; ENSMUSP00000090564; ENSMUSG00000069805; Mus musculus. [Genome view]
GeneID14121.
KEGGmmu:14121.
NMPDRfig|10090.3.peg.28005.
UCSCuc007qxg.1. mouse.

Organism-specific databases

CTD14121.
MGIMGI:95492. Fbp1.

Phylogenomic databases

eggNOGroNOG08567.
HOGENOMHBG731261.
HOVERGENQ9QXD6.
InParanoidQ9QXD6.
OMATCLLVSE.
OrthoDBEOG9Z3905.
PhylomeDBQ9QXD6.

Enzyme and pathway databases

BRENDA3.1.3.11. 244.

Gene expression databases

ArrayExpressQ9QXD6.
BgeeQ9QXD6.
CleanExMM_FBP1.
GenevestigatorQ9QXD6.
GermOnlineENSMUSG00000069805. Mus musculus.

Family and domain databases

InterProIPR000146. Fructose_bisphosphatase.
IPR020548. Fructose_bisphosphatase_AS.
[Graphical view]
PANTHERPTHR11556. In_FB_phphtase. 1 hit.
PfamPF00316. FBPase. 1 hit.
[Graphical view]
PRINTSPR00115. F16BPHPHTASE.
PROSITEPS00124. FBPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio285192.
SOURCESearch...

Entry information

Entry nameF16P1_MOUSE
AccessionPrimary (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 19, 2010
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents