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P25114

- F264_RAT

UniProt

P25114 - F264_RAT

Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4

Gene

Pfkfb4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Synthesis and degradation of fructose 2,6-bisphosphate.

    Catalytic activityi

    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 regulationi

    The most important regulatory mechanism of these opposing activities is by phosphorylation and dephosphorylation of the enzyme.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei79 – 791Fructose 6-phosphateBy similarity
    Binding sitei103 – 1031Fructose 6-phosphateBy similarity
    Active sitei129 – 1291Sequence Analysis
    Binding sitei131 – 1311Fructose 6-phosphateBy similarity
    Binding sitei137 – 1371Fructose 6-phosphateBy similarity
    Active sitei159 – 1591Sequence Analysis
    Binding sitei173 – 1731Fructose 6-phosphateBy similarity
    Binding sitei194 – 1941Fructose 6-phosphateBy similarity
    Binding sitei198 – 1981Fructose 6-phosphateBy similarity
    Binding sitei256 – 2561Fructose 2,6-bisphosphateBy similarity
    Active sitei257 – 2571Tele-phosphohistidine intermediate1 Publication
    Binding sitei263 – 2631Fructose 2,6-bisphosphateBy similarity
    Binding sitei269 – 2691Fructose 2,6-bisphosphate; via amide nitrogen
    Active sitei326 – 3261Proton donor/acceptor1 Publication
    Binding sitei337 – 3371Fructose 2,6-bisphosphate
    Binding sitei351 – 3511Fructose 2,6-bisphosphate
    Binding sitei355 – 3551Fructose 2,6-bisphosphate
    Binding sitei366 – 3661Fructose 2,6-bisphosphate
    Active sitei391 – 3911Proton donor/acceptorBy similarity
    Binding sitei392 – 3921Fructose 2,6-bisphosphate
    Binding sitei396 – 3961Fructose 2,6-bisphosphate
    Binding sitei428 – 4281ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi46 – 549ATP
    Nucleotide bindingi168 – 1736ATP
    Nucleotide bindingi348 – 3514ATPBy similarity
    Nucleotide bindingi392 – 3965ATPBy similarity

    GO - Molecular functioni

    1. 6-phosphofructo-2-kinase activity Source: RGD
    2. ATP binding Source: UniProtKB-KW
    3. fructose-2,6-bisphosphate 2-phosphatase activity Source: RGD

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. dephosphorylation Source: GOC
    3. fructose 2,6-bisphosphate metabolic process Source: InterPro
    4. fructose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.46. 5301.
    ReactomeiREACT_225694. Glycolysis.
    SABIO-RKP25114.

    Names & Taxonomyi

    Protein namesi
    Recommended 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:
    Fructose-2,6-bisphosphatase (EC:3.1.3.46)
    Gene namesi
    Name:Pfkfb4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi3310. Pfkfb4.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4694696-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4PRO_0000179971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei29 – 291Phosphoserine; by PKCSequence Analysis
    Modified residuei444 – 4441Phosphothreonine; by PKCSequence Analysis

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Tissue specificityi

    Testis.

    Gene expression databases

    GenevestigatoriP25114.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    DIPiDIP-2904N.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 456
    Helixi52 – 6514
    Beta strandi70 – 745
    Helixi75 – 839
    Helixi89 – 924
    Helixi97 – 11923
    Beta strandi124 – 1307
    Helixi135 – 14814
    Beta strandi151 – 1577
    Helixi162 – 17211
    Turni173 – 1753
    Turni177 – 1815
    Helixi184 – 19916
    Turni207 – 2126
    Beta strandi215 – 2184
    Turni220 – 2223
    Beta strandi225 – 2284
    Helixi233 – 24210
    Beta strandi252 – 2565
    Helixi261 – 2655
    Helixi276 – 29217
    Beta strandi298 – 3014
    Helixi305 – 3117
    Beta strandi314 – 3163
    Beta strandi318 – 3203
    Helixi322 – 3243
    Helixi330 – 3323
    Helixi337 – 3437
    Helixi345 – 3539
    Turni355 – 3573
    Helixi366 – 38217
    Beta strandi384 – 3907
    Helixi392 – 40211
    Turni407 – 4093
    Helixi410 – 4123
    Beta strandi419 – 4257
    Beta strandi427 – 43610
    Helixi458 – 4614
    Turni462 – 4643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BIFX-ray2.00A1-469[»]
    2BIFX-ray2.40A/B1-469[»]
    3BIFX-ray2.30A2-469[»]
    ProteinModelPortaliP25114.
    SMRiP25114. Positions 6-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25114.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 2492496-phosphofructo-2-kinaseAdd
    BLAST
    Regioni250 – 469220Fructose-2,6-bisphosphataseAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0406.
    GeneTreeiENSGT00390000018751.
    HOGENOMiHOG000181112.
    HOVERGENiHBG005628.
    InParanoidiP25114.
    KOiK01103.
    OMAiTSPDYRG.
    OrthoDBiEOG7M3J03.
    PhylomeDBiP25114.
    TreeFamiTF313541.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003094. 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]
    PANTHERiPTHR10606. PTHR10606. 1 hit.
    PfamiPF01591. 6PF2K. 1 hit.
    PF00300. His_Phos_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000709. 6PFK_2-Ptase. 1 hit.
    PRINTSiPR00991. 6PFRUCTKNASE.
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF53254. SSF53254. 1 hit.
    PROSITEiPS00175. PG_MUTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25114-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPRELTQN PLKKIWMPYS NGRPALHASQ RGVCMTNCPT LIVMVGLPAR    50
    GKTYISKKLT RYLNWIGVPT REFNVGQYRR DMVKTYKSFE FFLPDNEEGL 100
    KIRKQCALAA LNDVRKFLSE EGGHVAVFDA TNTTRERRAM IFNFGEQNGY 150
    KTFFVESICV DPEVIAANIV QVKLGSPDYV NRDSDEATED FMRRIECYEN 200
    SYESLDEEQD RDLSYIKIMD VGQSYVVNRV ADHIQSRIVY YLMNIHVTPR 250
    SIYLCRHGES ELNLKGRIGG DPGLSPRGRE FSKHLAQFIS DQNIKDLKVW 300
    TSQMKRTIQT AEALSVPYEQ WKVLNEIDAG VCEEMTYEEI QDHYPLEFAL 350
    RDQDKYRYRY PKGESYEDLV QRLEPVIMEL ERQENVLVIC HQAVMRCLLA 400
    YFLDKAAEEL PYLKCPLHTV LKLTPVAYGC KVESIFLNVA AVNTHRDRPQ 450
    NVDISRPSEE ALVTVPAHQ 469
    Length:469
    Mass (Da):54,155
    Last modified:January 23, 2007 - v3
    Checksum:iE3D0AF34D3A09CA6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64797 mRNA. Translation: AAA41163.1.
    PIRiA40800.
    RefSeqiNP_062206.1. NM_019333.1.
    UniGeneiRn.90092.

    Genome annotation databases

    EnsembliENSRNOT00000028039; ENSRNOP00000028039; ENSRNOG00000020656.
    GeneIDi54283.
    KEGGirno:54283.
    UCSCiRGD:3310. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64797 mRNA. Translation: AAA41163.1 .
    PIRi A40800.
    RefSeqi NP_062206.1. NM_019333.1.
    UniGenei Rn.90092.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BIF X-ray 2.00 A 1-469 [» ]
    2BIF X-ray 2.40 A/B 1-469 [» ]
    3BIF X-ray 2.30 A 2-469 [» ]
    ProteinModelPortali P25114.
    SMRi P25114. Positions 6-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-2904N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000028039 ; ENSRNOP00000028039 ; ENSRNOG00000020656 .
    GeneIDi 54283.
    KEGGi rno:54283.
    UCSCi RGD:3310. rat.

    Organism-specific databases

    CTDi 5210.
    RGDi 3310. Pfkfb4.

    Phylogenomic databases

    eggNOGi COG0406.
    GeneTreei ENSGT00390000018751.
    HOGENOMi HOG000181112.
    HOVERGENi HBG005628.
    InParanoidi P25114.
    KOi K01103.
    OMAi TSPDYRG.
    OrthoDBi EOG7M3J03.
    PhylomeDBi P25114.
    TreeFami TF313541.

    Enzyme and pathway databases

    BRENDAi 3.1.3.46. 5301.
    Reactomei REACT_225694. Glycolysis.
    SABIO-RK P25114.

    Miscellaneous databases

    EvolutionaryTracei P25114.
    NextBioi 610862.
    PROi P25114.

    Gene expression databases

    Genevestigatori P25114.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003094. 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 ]
    PANTHERi PTHR10606. PTHR10606. 1 hit.
    Pfami PF01591. 6PF2K. 1 hit.
    PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000709. 6PFK_2-Ptase. 1 hit.
    PRINTSi PR00991. 6PFRUCTKNASE.
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF53254. SSF53254. 1 hit.
    PROSITEi PS00175. PG_MUTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiF264_RAT
    AccessioniPrimary (citable) accession number: P25114
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3