Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P25114

- F264_RAT

UniProt

P25114 - F264_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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

ExpressionAtlasiP25114. baseline.
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 – 456Combined sources
Helixi52 – 6514Combined sources
Beta strandi70 – 745Combined sources
Helixi75 – 839Combined sources
Helixi89 – 924Combined sources
Helixi97 – 11923Combined sources
Beta strandi124 – 1307Combined sources
Helixi135 – 14814Combined sources
Beta strandi151 – 1577Combined sources
Helixi162 – 17211Combined sources
Turni173 – 1753Combined sources
Turni177 – 1815Combined sources
Helixi184 – 19916Combined sources
Turni207 – 2126Combined sources
Beta strandi215 – 2184Combined sources
Turni220 – 2223Combined sources
Beta strandi225 – 2284Combined sources
Helixi233 – 24210Combined sources
Beta strandi252 – 2565Combined sources
Helixi261 – 2655Combined sources
Helixi276 – 29217Combined sources
Beta strandi298 – 3014Combined sources
Helixi305 – 3117Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi318 – 3203Combined sources
Helixi322 – 3243Combined sources
Helixi330 – 3323Combined sources
Helixi337 – 3437Combined sources
Helixi345 – 3539Combined sources
Turni355 – 3573Combined sources
Helixi366 – 38217Combined sources
Beta strandi384 – 3907Combined sources
Helixi392 – 40211Combined sources
Turni407 – 4093Combined sources
Helixi410 – 4123Combined sources
Beta strandi419 – 4257Combined sources
Beta strandi427 – 43610Combined sources
Helixi458 – 4614Combined sources
Turni462 – 4643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MASPRELTQN PLKKIWMPYS NGRPALHASQ RGVCMTNCPT LIVMVGLPAR
60 70 80 90 100
GKTYISKKLT RYLNWIGVPT REFNVGQYRR DMVKTYKSFE FFLPDNEEGL
110 120 130 140 150
KIRKQCALAA LNDVRKFLSE EGGHVAVFDA TNTTRERRAM IFNFGEQNGY
160 170 180 190 200
KTFFVESICV DPEVIAANIV QVKLGSPDYV NRDSDEATED FMRRIECYEN
210 220 230 240 250
SYESLDEEQD RDLSYIKIMD VGQSYVVNRV ADHIQSRIVY YLMNIHVTPR
260 270 280 290 300
SIYLCRHGES ELNLKGRIGG DPGLSPRGRE FSKHLAQFIS DQNIKDLKVW
310 320 330 340 350
TSQMKRTIQT AEALSVPYEQ WKVLNEIDAG VCEEMTYEEI QDHYPLEFAL
360 370 380 390 400
RDQDKYRYRY PKGESYEDLV QRLEPVIMEL ERQENVLVIC HQAVMRCLLA
410 420 430 440 450
YFLDKAAEEL PYLKCPLHTV LKLTPVAYGC KVESIFLNVA AVNTHRDRPQ
460
NVDISRPSEE ALVTVPAHQ
Length:469
Mass (Da):54,155
Last modified:January 23, 2007 - v3
Checksum:iE3D0AF34D3A09CA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64797 mRNA. Translation: AAA41163.1.
PIRiA40800.
RefSeqiNP_062206.1. NM_019333.1.
XP_008764785.1. XM_008766563.1.
UniGeneiRn.90092.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64797 mRNA. Translation: AAA41163.1 .
PIRi A40800.
RefSeqi NP_062206.1. NM_019333.1.
XP_008764785.1. XM_008766563.1.
UniGenei Rn.90092.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

ExpressionAtlasi P25114. baseline.
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: November 26, 2014
This is version 133 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