[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Testis; PubMed=1651918 [NCBI, ExPASy, EBI, Israel, Japan] Sakata J., Abe Y., Uyeda K.; "Molecular cloning of the DNA and expression and characterization of rat testes fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase."; J. Biol. Chem. 266:15764-15770(1991).
[2]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). TISSUE=Testis; DOI=10.1016/S0969-2126(96)00109-8; PubMed=8805587 [NCBI, ExPASy, EBI, Israel, Japan] Hasemann C.A., Istvan E.S., Uyeda K., Deisenhofer J.; "The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies."; Structure 4:1017-1029(1996).
[3]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT ALA-257. TISSUE=Testis; DOI=10.1074/jbc.274.4.2176; PubMed=9890980 [NCBI, ExPASy, EBI, Israel, Japan] Yuen M.H., Mizuguchi H., Lee Y.H., Cook P.F., Uyeda K., Hasemann C.A.; "Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities."; J. Biol. Chem. 274:2176-2184(1999).

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: The most important regulatory mechanism of these opposing activities is by phosphorylation and dephosphorylation of the enzyme.
SUBUNIT: Homodimer.
INTERACTION:
Self; NbExp=1; IntAct=EBI-728132, EBI-728132;
TISSUE SPECIFICITY: Testis.
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

M64797; AAA41163.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A40800; A40800.

NP_062206.1; -.

3D structure databases

PDB

1BIF; X-ray; 2.00 A; A=1-469.	[ExPASy / RCSB / EBI]
2BIF; X-ray; 2.40 A; A/B=1-469.	[ExPASy / RCSB / EBI]
3BIF; X-ray; 2.30 A; A=1-469.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BIF; -.
2BIF; -.
3BIF; -.

ModBase

P25114.

Protein-protein interaction databases

IntAct

P25114; -.

Organism-specific databases

RGD

3310; Pfkfb4.

Gene expression databases

ArrayExpress

P25114; -.

GermOnline

ENSRNOG00000020656; Rattus norvegicus.

Ontologies

GO:0003873;	Molecular function: 6-phosphofructo-2-kinase activity (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004331;	Molecular function: fructose-2,6-bisphosphate 2-phosphatase activity (inferred from electronic annotation from EC).
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 electronic annotation from InterPro).
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

ENSRNOG00000020656; Rattus norvegicus. [Contig view]

GeneID

54283; -.

KEGG

rno:54283; -.

Phylogenomic databases

HOVERGEN

P25114; -.

Other

LinkHub

P25114; -.

NextBio

610862; -.

UniRef

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

Keywords

3D-structure; ATP-binding; 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`	`2 469`	`468`	`6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4.`	`PRO_0000179971`
`NP_BIND`	`46 53`	`8`	`ATP (Potential).`
`REGION`	`2 249`	`248`	`6-phosphofructo-2-kinase.`
`REGION`	`250 469`	`220`	`Fructose-2,6-bisphosphatase.`
`ACT_SITE`	`129 129`		`Potential.`
`ACT_SITE`	`159 159`		`Potential.`
`ACT_SITE`	`257 257`		`Tele-phosphohistidine intermediate.`
`ACT_SITE`	`326 326`		`Potential.`
`ACT_SITE`	`391 391`		`Proton donor (By similarity).`
`BINDING`	`103 103`		`Fructose-6-phosphate (By similarity).`
`BINDING`	`194 194`		`Fructose-6-phosphate (By similarity).`
`MOD_RES`	`29 29`		`Phosphoserine; by PKC (Potential).`
`MOD_RES`	`444 444`		`Phosphothreonine; by PKC (Potential).`
`STRAND`	`40 45`	`6`
`HELIX`	`52 65`	`14`
`STRAND`	`70 74`	`5`
`HELIX`	`75 83`	`9`
`HELIX`	`89 92`	`4`
`HELIX`	`97 119`	`23`
`STRAND`	`124 130`	`7`
`HELIX`	`135 148`	`14`
`STRAND`	`151 157`	`7`
`HELIX`	`162 172`	`11`
`TURN`	`173 175`	`3`
`TURN`	`177 181`	`5`
`HELIX`	`184 199`	`16`
`TURN`	`207 212`	`6`
`STRAND`	`215 218`	`4`
`TURN`	`220 222`	`3`
`STRAND`	`223 228`	`6`
`HELIX`	`233 242`	`10`
`STRAND`	`252 256`	`5`
`HELIX`	`261 265`	`5`
`HELIX`	`276 292`	`17`
`STRAND`	`298 301`	`4`
`HELIX`	`305 311`	`7`
`STRAND`	`314 316`	`3`
`HELIX`	`322 324`	`3`
`HELIX`	`330 332`	`3`
`HELIX`	`337 343`	`7`
`HELIX`	`345 353`	`9`
`TURN`	`355 357`	`3`
`HELIX`	`366 382`	`17`
`STRAND`	`384 390`	`7`
`HELIX`	`392 402`	`11`
`TURN`	`407 409`	`3`
`HELIX`	`410 412`	`3`
`STRAND`	`419 425`	`7`
`STRAND`	`427 436`	`10`
`HELIX`	`458 461`	`4`

Sequence information

Length: 469 AA [This is the length of the unprocessed precursor]

Molecular weight: 54155 Da [This is the MW of the unprocessed precursor]

CRC64: E3D0AF34D3A09CA6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASPRELTQN PLKKIWMPYS NGRPALHASQ RGVCMTNCPT LIVMVGLPAR GKTYISKKLT 

        70         80         90        100        110        120 
RYLNWIGVPT REFNVGQYRR DMVKTYKSFE FFLPDNEEGL KIRKQCALAA LNDVRKFLSE 

       130        140        150        160        170        180 
EGGHVAVFDA TNTTRERRAM IFNFGEQNGY KTFFVESICV DPEVIAANIV QVKLGSPDYV 

       190        200        210        220        230        240 
NRDSDEATED FMRRIECYEN SYESLDEEQD RDLSYIKIMD VGQSYVVNRV ADHIQSRIVY 

       250        260        270        280        290        300 
YLMNIHVTPR SIYLCRHGES ELNLKGRIGG DPGLSPRGRE FSKHLAQFIS DQNIKDLKVW 

       310        320        330        340        350        360 
TSQMKRTIQT AEALSVPYEQ WKVLNEIDAG VCEEMTYEEI QDHYPLEFAL RDQDKYRYRY 

       370        380        390        400        410        420 
PKGESYEDLV QRLEPVIMEL ERQENVLVIC HQAVMRCLLA YFLDKAAEEL PYLKCPLHTV 

       430        440        450        460 
LKLTPVAYGC KVESIFLNVA AVNTHRDRPQ NVDISRPSEE ALVTVPAHQ

P25114 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