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Protein

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

Gene

Pfkfb4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei79Fructose 6-phosphate1 Publication1
Binding sitei103Fructose 6-phosphateBy similarity1
Active sitei129Sequence analysis1
Binding sitei131Fructose 6-phosphate1 Publication1
Binding sitei137Fructose 6-phosphate1 Publication1
Active sitei159Sequence analysis1
Binding sitei173Fructose 6-phosphateBy similarity1
Binding sitei194Fructose 6-phosphateBy similarity1
Binding sitei198Fructose 6-phosphate1 Publication1
Binding sitei256Fructose 2,6-bisphosphateBy similarity1
Active sitei257Tele-phosphohistidine intermediate1 Publication1
Binding sitei263Fructose 2,6-bisphosphateBy similarity1
Binding sitei269Fructose 2,6-bisphosphate; via amide nitrogen1 Publication1
Binding sitei306Fructose 2,6-bisphosphateBy similarity1
Active sitei326Proton donor/acceptor1 Publication1
Binding sitei337Fructose 2,6-bisphosphate1 Publication1
Binding sitei351Fructose 2,6-bisphosphate1 Publication1
Binding sitei355Fructose 2,6-bisphosphate1 Publication1
Binding sitei366Fructose 2,6-bisphosphate1 Publication1
Sitei391Transition state stabilizerBy similarity1
Binding sitei392Fructose 2,6-bisphosphate1 Publication1
Binding sitei396Fructose 2,6-bisphosphate1 Publication1
Binding sitei428ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 54ATP1 Publication9
Nucleotide bindingi168 – 173ATP1 Publication6
Nucleotide bindingi348 – 351ATPBy similarity4
Nucleotide bindingi392 – 396ATPBy similarity5

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.105. 5301.
3.1.3.46. 5301.
ReactomeiR-RNO-70171. 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
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi3310. Pfkfb4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001799711 – 4696-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4Add BLAST469

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei29Phosphoserine; by PKCSequence analysis1
Modified residuei444Phosphothreonine; by PKCSequence analysis1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP25114.

Expressioni

Tissue specificityi

Testis.

Gene expression databases

BgeeiENSRNOG00000020656.
ExpressionAtlasiP25114. differential.
GenevisibleiP25114. RN.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

DIPiDIP-2904N.
STRINGi10116.ENSRNOP00000028039.

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 45Combined sources6
Helixi52 – 65Combined sources14
Beta strandi70 – 74Combined sources5
Helixi75 – 83Combined sources9
Helixi89 – 92Combined sources4
Helixi97 – 119Combined sources23
Beta strandi124 – 130Combined sources7
Helixi135 – 148Combined sources14
Beta strandi151 – 157Combined sources7
Helixi162 – 172Combined sources11
Turni173 – 175Combined sources3
Turni177 – 181Combined sources5
Helixi184 – 199Combined sources16
Turni207 – 212Combined sources6
Beta strandi215 – 218Combined sources4
Turni220 – 222Combined sources3
Beta strandi225 – 228Combined sources4
Helixi233 – 242Combined sources10
Beta strandi252 – 256Combined sources5
Helixi261 – 265Combined sources5
Helixi276 – 292Combined sources17
Beta strandi298 – 301Combined sources4
Helixi305 – 311Combined sources7
Beta strandi314 – 316Combined sources3
Beta strandi318 – 320Combined sources3
Helixi322 – 324Combined sources3
Helixi330 – 332Combined sources3
Helixi337 – 343Combined sources7
Helixi345 – 353Combined sources9
Turni355 – 357Combined sources3
Helixi366 – 382Combined sources17
Beta strandi384 – 390Combined sources7
Helixi392 – 402Combined sources11
Turni407 – 409Combined sources3
Helixi410 – 412Combined sources3
Beta strandi419 – 425Combined sources7
Beta strandi427 – 436Combined sources10
Helixi458 – 461Combined sources4
Turni462 – 464Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP25114.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 2496-phosphofructo-2-kinaseAdd BLAST249
Regioni250 – 469Fructose-2,6-bisphosphataseAdd BLAST220

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP25114.
KOiK19030.
OMAiDCSNDEA.
PhylomeDBiP25114.
TreeFamiTF313541.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
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]
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_008766563.2.
XP_017459205.1. XM_017603716.1.
UniGeneiRn.90092.

Genome annotation databases

EnsembliENSRNOT00000028039; ENSRNOP00000028039; ENSRNOG00000020656.
ENSRNOT00000090164; ENSRNOP00000074158; ENSRNOG00000020656.
GeneIDi100911725.
54283.
KEGGirno:54283.
UCSCiRGD:3310. rat.

Cross-referencesi

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_008766563.2.
XP_017459205.1. XM_017603716.1.
UniGeneiRn.90092.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-2904N.
STRINGi10116.ENSRNOP00000028039.

Proteomic databases

PaxDbiP25114.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028039; ENSRNOP00000028039; ENSRNOG00000020656.
ENSRNOT00000090164; ENSRNOP00000074158; ENSRNOG00000020656.
GeneIDi100911725.
54283.
KEGGirno:54283.
UCSCiRGD:3310. rat.

Organism-specific databases

CTDi5210.
RGDi3310. Pfkfb4.

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP25114.
KOiK19030.
OMAiDCSNDEA.
PhylomeDBiP25114.
TreeFamiTF313541.

Enzyme and pathway databases

BRENDAi2.7.1.105. 5301.
3.1.3.46. 5301.
ReactomeiR-RNO-70171. Glycolysis.
SABIO-RKP25114.

Miscellaneous databases

EvolutionaryTraceiP25114.
PROiP25114.

Gene expression databases

BgeeiENSRNOG00000020656.
ExpressionAtlasiP25114. differential.
GenevisibleiP25114. RN.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
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]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 148 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.