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P25114 (F264_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

Short name=6PF-2-K/Fru-2,6-P2ase 4
Short name=PFK/FBPase 4
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase testis-type isozyme

Including the following 2 domains:

  1. 6-phosphofructo-2-kinase
    EC=2.7.1.105
  2. Fructose-2,6-bisphosphatase
    EC=3.1.3.46
Gene names
Name:Pfkfb4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activity

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

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 structure

Homodimer. Ref.3

Tissue specificity

Testis.

Sequence similarities

In the C-terminal section; belongs to the phosphoglycerate mutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4694696-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4
PRO_0000179971

Regions

Nucleotide binding46 – 549ATP
Nucleotide binding168 – 1736ATP
Nucleotide binding348 – 3514ATP By similarity
Nucleotide binding392 – 3965ATP By similarity
Region1 – 2492496-phosphofructo-2-kinase
Region250 – 469220Fructose-2,6-bisphosphatase

Sites

Active site1291 Potential
Active site1591 Potential
Active site2571Tele-phosphohistidine intermediate Ref.3
Active site3261Proton donor/acceptor Ref.3
Active site3911Proton donor/acceptor By similarity
Binding site791Fructose 6-phosphate By similarity
Binding site1031Fructose 6-phosphate By similarity
Binding site1311Fructose 6-phosphate By similarity
Binding site1371Fructose 6-phosphate By similarity
Binding site1731Fructose 6-phosphate By similarity
Binding site1941Fructose 6-phosphate By similarity
Binding site1981Fructose 6-phosphate By similarity
Binding site2561Fructose 2,6-bisphosphate By similarity
Binding site2631Fructose 2,6-bisphosphate By similarity
Binding site2691Fructose 2,6-bisphosphate; via amide nitrogen
Binding site3371Fructose 2,6-bisphosphate
Binding site3511Fructose 2,6-bisphosphate
Binding site3551Fructose 2,6-bisphosphate
Binding site3661Fructose 2,6-bisphosphate
Binding site3921Fructose 2,6-bisphosphate
Binding site3961Fructose 2,6-bisphosphate
Binding site4281ATP

Amino acid modifications

Modified residue291Phosphoserine; by PKC Potential
Modified residue4441Phosphothreonine; by PKC Potential

Secondary structure

........................................................................... 469
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25114 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E3D0AF34D3A09CA6

FASTA46954,155
        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 

« Hide

References

[1]"Molecular cloning of the DNA and expression and characterization of rat testes fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase."
Sakata J., Abe Y., Uyeda K.
J. Biol. Chem. 266:15764-15770(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies."
Hasemann C.A., Istvan E.S., Uyeda K., Deisenhofer J.
Structure 4:1017-1029(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.
Tissue: Testis.
[3]"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."
Yuen M.H., Mizuguchi H., Lee Y.H., Cook P.F., Uyeda K., Hasemann C.A.
J. Biol. Chem. 274:2176-2184(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT ALA-257 IN COMPLEX WITH ATP ANALOG; FRUCTOSE 6-PHOSPHATE AND PHOSPHATE ION, SUBUNIT, ACTIVE SITE.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64797 mRNA. Translation: AAA41163.1.
PIRA40800.
RefSeqNP_062206.1. NM_019333.1.
UniGeneRn.90092.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BIFX-ray2.00A1-469[»]
2BIFX-ray2.40A/B1-469[»]
3BIFX-ray2.30A2-469[»]
ProteinModelPortalP25114.
SMRP25114. Positions 6-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-2904N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000028039; ENSRNOP00000028039; ENSRNOG00000020656.
GeneID54283.
KEGGrno:54283.
UCSCRGD:3310. rat.

Organism-specific databases

CTD5210.
RGD3310. Pfkfb4.

Phylogenomic databases

eggNOGCOG0406.
GeneTreeENSGT00390000018751.
HOGENOMHOG000181112.
HOVERGENHBG005628.
InParanoidP25114.
KOK01103.
OMATSPDYRG.
OrthoDBEOG7M3J03.
PhylomeDBP25114.
TreeFamTF313541.

Enzyme and pathway databases

BRENDA3.1.3.46. 5301.
SABIO-RKP25114.

Gene expression databases

GenevestigatorP25114.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
[Graphical view]
PANTHERPTHR10606. PTHR10606. 1 hit.
PfamPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PIRSFPIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSPR00991. 6PFRUCTKNASE.
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25114.
NextBio610862.
PROP25114.

Entry information

Entry nameF264_RAT
AccessionPrimary (citable) accession number: P25114
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references