[1]	NUCLEOTIDE SEQUENCE (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. STRAIN=Wistar; TISSUE=Liver; DOI=10.1016/0014-5793(87)80476-3; PubMed=2856848 [NCBI, ExPASy, EBI, Israel, Japan] Darville M.I., Crepin K.M., Vandekerckhove J., van Damme J., Octave J.-N., Rider M.H., Marchand M.J., Hue L., Rousseau G.G.; "Complete nucleotide sequence coding for rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase derived from a cDNA clone."; FEBS Lett. 224:317-321(1987).
[2]	NUCLEOTIDE SEQUENCE (ISOFORM 1). STRAIN=Sprague-Dawley; DOI=10.1016/0006-291X(87)90364-0; PubMed=3032183 [NCBI, ExPASy, EBI, Israel, Japan] Colosa A.D., Lively M.O., El-Maghrabi M.R., Pilkis S.J.; "Isolation of a cDNA clone for rat liver 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase."; Biochem. Biophys. Res. Commun. 143:1092-1098(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). STRAIN=Wistar; TISSUE=Liver; PubMed=2547611 [NCBI, ExPASy, EBI, Israel, Japan] Crepin K.M., Darville M.I., Hue L., Rousseau G.G.; "Characterization of distinct mRNAs coding for putative isozymes of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."; Eur. J. Biochem. 183:433-440(1989).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Liver; PubMed=2848802 [NCBI, ExPASy, EBI, Israel, Japan] Colosia A.D., Marker A.J., Lange A.J., El-Maghrabi M.R., Granner D.K., Tauler A., Pilkis J., Pilkis S.J.; "Induction of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase mRNA by refeeding and insulin."; J. Biol. Chem. 263:18669-18677(1988).
[5]	PROTEIN SEQUENCE (ISOFORM 1). TISSUE=Liver; PubMed=2826464 [NCBI, ExPASy, EBI, Israel, Japan] Lively M.O., El-Maghrabi M.R., Pilkis J., D'Angelo G., Colosia A.D., Ciavola J.A., Fraser B.A., Pilkis S.J.; "Complete amino acid sequence of rat liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."; J. Biol. Chem. 263:839-849(1988).
[6]	NUCLEOTIDE SEQUENCE (ISOFORM 2). STRAIN=Wistar; TISSUE=Liver; PubMed=2557826 [NCBI, ExPASy, EBI, Israel, Japan] Crepin K.M., Darville M.I., Michel A., Hue L., Rousseau G.G.; "Cloning and expression in Escherichia coli of a rat hepatoma cell cDNA coding for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."; Biochem. J. 264:151-160(1989).
[7]	PROTEIN SEQUENCE OF 220-267. TISSUE=Liver; PubMed=3040762 [NCBI, ExPASy, EBI, Israel, Japan] Pilkis S.J., Lively M.O., El-Maghrabi M.R.; "Active site sequence of hepatic fructose-2,6-bisphosphatase. Homology in primary structure with phosphoglycerate mutase."; J. Biol. Chem. 262:12672-12675(1987).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32 (ISOFORM 1), AND PROTEIN SEQUENCE OF 2-10 (ISOFORM 2). PubMed=2549541 [NCBI, ExPASy, EBI, Israel, Japan] Darville M.I., Crepin K.M., Hue L., Rousseau G.G.; "5' flanking sequence and structure of a gene encoding rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."; Proc. Natl. Acad. Sci. U.S.A. 86:6543-6547(1989).
[9]	DOMAINS. PubMed=2557623 [NCBI, ExPASy, EBI, Israel, Japan] Bazan J.F., Fletterick R.J., Pilkis S.J.; "Evolution of a bifunctional enzyme: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."; Proc. Natl. Acad. Sci. U.S.A. 86:9642-9646(1989).
[10]	FRUCTOSE-6-P BINDING SITES. PubMed=2539378 [NCBI, ExPASy, EBI, Israel, Japan] Kitamura K., Uyeda K., Hartman F.C., Kangawa K., Matsuo H.; "Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Identification of fructose 6-phosphate binding site."; J. Biol. Chem. 264:6344-6348(1989).
[11]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). TISSUE=Liver; DOI=10.1021/bi9600613; PubMed=8634242 [NCBI, ExPASy, EBI, Israel, Japan] Lee Y.-H., Ogata C., Pflugrath J.W., Levitt D.G., Sarma R., Banaszak L.J., Pilkis S.J.; "Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases."; Biochemistry 35:6010-6019(1996).
[12]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 251-441. DOI=10.1038/nsb0897-615; PubMed=9253407 [NCBI, ExPASy, EBI, Israel, Japan] Lee Y.-H., Olson T.W., Ogata C.M., Levitt D.G., Banaszak L.J., Lange A.J.; "Crystal structure of a trapped phosphoenzyme during a catalytic reaction."; Nat. Struct. Biol. 4:615-618(1997).

Comments

FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H₂O = D-fructose 6-phosphate + phosphate.
CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.
ENZYME REGULATION: Phosphorylation results in inhibition of the kinase activity.
SUBUNIT: Homodimer.
INTERACTION:
Self; NbExp=1; IntAct=EBI-709873, EBI-709873;
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID P07953-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID P07953-2

Features which should be applied to build the isoform sequence: VSP_004674.
TISSUE SPECIFICITY: Liver.
SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate mutase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y00702; CAA68694.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15579; CAA33606.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X15580; CAA33607.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26215; AAA02888.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26216; AAA02889.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04197; AAA79008.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M27886; AAA58780.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S11761; KIRTFB.

NP_036753.4; -.

3D structure databases

PDB

1C7Z; X-ray; 2.60 A; A/B=252-441.	[ExPASy / RCSB / EBI]
1C80; X-ray; 2.20 A; A/B=252-441.	[ExPASy / RCSB / EBI]
1C81; X-ray; 2.50 A; A=252-441.	[ExPASy / RCSB / EBI]
1FBT; X-ray; 2.00 A; A/B=252-441.	[ExPASy / RCSB / EBI]
1TIP; X-ray; 2.20 A; A/B=252-441.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1C7Z; -.
1C80; -.
1C81; -.
1FBT; -.
1TIP; -.

SMR

P07953; 42-470.

ModBase

P07953.

Protein-protein interaction databases

IntAct

P07953; -.

PTM databases

PhosphoSite

P07953; -.

Organism-specific databases

RGD

3307; Pfkfb1.

Gene expression databases

ArrayExpress

P07953; -.

GermOnline

ENSRNOG00000000165; Rattus norvegicus.

Ontologies

GO:0043540;	Cellular component: 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex (inferred from sequence or structural similarity from UniProtKB).
GO:0004331;	Molecular function: fructose-2,6-bisphosphate 2-phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0006003;	Biological process: fructose 2,6-bisphosphate metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003094; 6Pfruct_kin.
IPR013079; 6Phosfructo_kin.
IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
IPR001345; PG/BPGM_mutase.
IPR013078; PG_mutase.
Graphical view of domain structure.

PANTHER

PTHR10606; 6Pfruct_kin; 1.

Pfam

PF01591; 6PF2K; 1.
PF00300; PGAM; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000709; 6PFK_2-Ptase; 1.

PRINTS

PR00991; 6PFRUCTKNASE.

PROSITE

PS00175; PG_MUTASE; 1.

Genome annotation databases

Ensembl

ENSRNOG00000000165; Rattus norvegicus. [Contig view]

GeneID

24638; -.

KEGG

rno:24638; -.

Phylogenomic databases

HOVERGEN

P07953; -.

Other

LinkHub

P07953; -.

NextBio

603924; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Alternative splicing; ATP-binding; Direct protein sequencing; Hydrolase; Kinase; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 471`	`470`	`6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1.`	`PRO_0000179962`
`NP_BIND`	`49 56`	`8`	`ATP (By similarity).`
`REGION`	`2 250`	`249`	`6-phosphofructo-2-kinase.`
`REGION`	`251 471`	`221`	`Fructose-2,6-bisphosphatase.`
`ACT_SITE`	`131 131`		`Potential.`
`ACT_SITE`	`161 161`		`Potential.`
`ACT_SITE`	`259 259`		`Tele-phosphohistidine intermediate.`
`ACT_SITE`	`328 328`		`Potential.`
`ACT_SITE`	`393 393`		`Proton donor.`
`BINDING`	`105 105`		`Fructose-6-phosphate (By similarity).`
`BINDING`	`196 196`		`Fructose-6-phosphate (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine.`
`MOD_RES`	`33 33`		`Phosphoserine; by PKA.`
`VAR_SEQ`	`1 33`		`MSREMGELTQTRLQKIWIPHSSSSSVLQRRRGS -> MEEKASKRTA (in isoform 2).`	`VSP_004674`
`CONFLICT`	`135 135`		`T -> Y (in Ref. 3, 4 and 5).`
`CONFLICT`	`138 138`		`E -> F (in Ref. 3).`
`CONFLICT`	`257 257`		`Missing (in Ref. 7; AA sequence).`
`STRAND`	`254 258`	`5`
`HELIX`	`263 267`	`5`
`HELIX`	`278 293`	`16`
`STRAND`	`300 303`	`4`
`HELIX`	`307 314`	`8`
`TURN`	`315 317`	`3`
`STRAND`	`320 322`	`3`
`HELIX`	`324 326`	`3`
`HELIX`	`332 334`	`3`
`HELIX`	`339 345`	`7`
`HELIX`	`347 355`	`9`
`TURN`	`357 359`	`3`
`HELIX`	`368 383`	`16`
`STRAND`	`386 392`	`7`
`HELIX`	`394 404`	`11`
`TURN`	`409 411`	`3`
`HELIX`	`412 414`	`3`
`STRAND`	`421 428`	`8`
`STRAND`	`431 438`	`8`

Sequence information

Length: 471 AA [This is the length of the unprocessed precursor]

Molecular weight: 54763 Da [This is the MW of the unprocessed precursor]

CRC64: E307AF13945E0FCD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSREMGELTQ TRLQKIWIPH SSSSSVLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST 

        70         80         90        100        110        120 
KLTRYLNWIG TPTKVFNLGQ YRREAVSYRN YEFFRPDNTE AQLIRKQCAL AALKDVHKYL 

       130        140        150        160        170        180 
SREEGHVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPEIIAEN IKQVKLGSPD 

       190        200        210        220        230        240 
YIDCDQEKVL EDFLKRIECY EINYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHVQSRT 

       250        260        270        280        290        300 
AYYLMNIHVT PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IRSQGISSLK 

       310        320        330        340        350        360 
VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY 

       370        380        390        400        410        420 
RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH 

       430        440        450        460        470 
TVLKLTPVAY GCRVESIYLN VEAVNTHRDK PENVDITREA EEALDTVPAH Y

P07953 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools