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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1

Gene

Pfkfb1

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

Phosphorylation at Ser-33 inhibits the kinase and activates the bisphosphatase.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei82Fructose 6-phosphateBy similarity1
Binding sitei105Fructose 6-phosphateBy similarity1
Active sitei131Sequence analysis1
Binding sitei133Fructose 6-phosphateBy similarity1
Binding sitei139Fructose 6-phosphateBy similarity1
Active sitei161Sequence analysis1
Binding sitei175Fructose 6-phosphateBy similarity1
Binding sitei196Fructose 6-phosphateBy similarity1
Binding sitei200Fructose 6-phosphateBy similarity1
Binding sitei258Fructose 2,6-bisphosphateBy similarity1
Active sitei259Tele-phosphohistidine intermediate1 Publication1
Binding sitei265Fructose 2,6-bisphosphateBy similarity1
Binding sitei271Fructose 2,6-bisphosphate; via amide nitrogen1 Publication1
Binding sitei308Fructose 2,6-bisphosphateBy similarity1
Active sitei328Proton donor/acceptor1 Publication1
Binding sitei339Fructose 2,6-bisphosphate1 Publication1
Binding sitei353Fructose 2,6-bisphosphate1 Publication1
Binding sitei357Fructose 2,6-bisphosphate1 Publication1
Binding sitei368Fructose 2,6-bisphosphate1 Publication1
Sitei393Transition state stabilizerBy similarity1
Binding sitei394Fructose 2,6-bisphosphate1 Publication1
Binding sitei398Fructose 2,6-bisphosphate1 Publication1
Binding sitei430ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi49 – 57ATPBy similarity9
Nucleotide bindingi170 – 175ATPBy similarity6
Nucleotide bindingi350 – 353ATP1 Publication4
Nucleotide bindingi394 – 398ATP1 Publication5

GO - Molecular functioni

  • 6-phosphofructo-2-kinase activity Source: RGD
  • ATP binding Source: RGD
  • fructose-2,6-bisphosphate 2-phosphatase activity Source: UniProtKB
  • fructose-6-phosphate binding Source: RGD
  • identical protein binding Source: IntAct
  • kinase binding Source: RGD

GO - Biological processi

  • animal organ regeneration Source: RGD
  • canonical glycolysis Source: Reactome
  • carbohydrate phosphorylation Source: RGD
  • energy reserve metabolic process Source: Reactome
  • fructose 2,6-bisphosphate metabolic process Source: UniProtKB
  • fructose metabolic process Source: InterPro
  • gluconeogenesis Source: Reactome
  • intracellular signal transduction Source: Reactome
  • positive regulation of glucokinase activity Source: RGD
  • response to cAMP Source: RGD
  • response to glucagon Source: RGD
  • response to glucocorticoid Source: RGD
  • response to insulin Source: RGD
  • response to starvation Source: RGD
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-163358. PKA-mediated phosphorylation of key metabolic factors.
R-RNO-163767. PP2A-mediated dephosphorylation of key metabolic factors.
R-RNO-70171. Glycolysis.
R-RNO-70263. Gluconeogenesis.
SABIO-RKP07953.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
Short name:
6PF-2-K/Fru-2,6-P2ase 1
Short name:
PFK/FBPase 1
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase liver isozyme
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:Pfkfb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi3307. Pfkfb1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001799622 – 4716-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1Add BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei33Phosphoserine; by PKA1 Publication1
Modified residuei141PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07953.
PRIDEiP07953.

PTM databases

iPTMnetiP07953.
PhosphoSitePlusiP07953.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSRNOG00000000165.
ExpressionAtlasiP07953. baseline and differential.
GenevisibleiP07953. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-709873,EBI-709873

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • kinase binding Source: RGD

Protein-protein interaction databases

IntActiP07953. 2 interactors.
MINTiMINT-8147404.
STRINGi10116.ENSRNOP00000035212.

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi253 – 258Combined sources6
Helixi263 – 267Combined sources5
Helixi278 – 292Combined sources15
Beta strandi300 – 306Combined sources7
Helixi307 – 314Combined sources8
Turni315 – 317Combined sources3
Beta strandi321 – 323Combined sources3
Helixi324 – 326Combined sources3
Helixi332 – 334Combined sources3
Helixi339 – 345Combined sources7
Helixi347 – 355Combined sources9
Turni357 – 359Combined sources3
Helixi368 – 374Combined sources7
Helixi376 – 383Combined sources8
Beta strandi386 – 392Combined sources7
Helixi394 – 404Combined sources11
Turni409 – 411Combined sources3
Helixi412 – 414Combined sources3
Beta strandi421 – 428Combined sources8
Beta strandi431 – 438Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C7ZX-ray2.60A/B252-441[»]
1C80X-ray2.20A/B252-441[»]
1C81X-ray2.50A252-441[»]
1FBTX-ray2.00A/B252-441[»]
1TIPX-ray2.20A/B252-441[»]
ProteinModelPortaliP07953.
SMRiP07953.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07953.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 2506-phosphofructo-2-kinaseAdd BLAST249
Regioni251 – 471Fructose-2,6-bisphosphataseAdd BLAST221

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP07953.
KOiK19028.
OMAiDYIDCDQ.
OrthoDBiEOG091G0A43.
PhylomeDBiP07953.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P07953-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSREMGELTQ TRLQKIWIPH SSSSSVLQRR RGSSIPQFTN SPTMVIMVGL
60 70 80 90 100
PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYRN YEFFRPDNTE
110 120 130 140 150
AQLIRKQCAL AALKDVHKYL SREEGHVAVF DATNTTRERR SLILQFAKEH
160 170 180 190 200
GYKVFFIESI CNDPEIIAEN IKQVKLGSPD YIDCDQEKVL EDFLKRIECY
210 220 230 240 250
EINYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHVQSRT AYYLMNIHVT
260 270 280 290 300
PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IRSQGISSLK
310 320 330 340 350
VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF
360 370 380 390 400
ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL
410 420 430 440 450
LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCRVESIYLN VEAVNTHRDK
460 470
PENVDITREA EEALDTVPAH Y
Length:471
Mass (Da):54,763
Last modified:January 23, 2007 - v3
Checksum:iE307AF13945E0FCD
GO
Isoform 2 (identifier: P07953-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSREMGELTQTRLQKIWIPHSSSSSVLQRRRGS → MEEKASKRTA

Show »
Length:448
Mass (Da):52,070
Checksum:i3DCD00D54929917D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti135T → Y (PubMed:2547611).Curated1
Sequence conflicti135T → Y (PubMed:2848802).Curated1
Sequence conflicti135T → Y (PubMed:2826464).Curated1
Sequence conflicti138E → F (PubMed:2547611).Curated1
Sequence conflicti257Missing AA sequence (PubMed:3040762).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0046741 – 33MSREM…RRRGS → MEEKASKRTA in isoform 2. 1 PublicationAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00702 mRNA. Translation: CAA68694.1.
X15579 mRNA. Translation: CAA33606.1.
X15580 mRNA. Translation: CAA33607.1.
M26215 Genomic DNA. Translation: AAA02888.2.
M26216 Genomic DNA. Translation: AAA02889.1.
J04197 mRNA. Translation: AAA79008.1.
M27886 Genomic DNA. Translation: AAA58780.1.
PIRiS11761. KIRTFB.
RefSeqiNP_036753.4. NM_012621.4. [P07953-1]
UniGeneiRn.10115.

Genome annotation databases

EnsembliENSRNOT00000033656; ENSRNOP00000035212; ENSRNOG00000000165. [P07953-1]
GeneIDi24638.
KEGGirno:24638.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00702 mRNA. Translation: CAA68694.1.
X15579 mRNA. Translation: CAA33606.1.
X15580 mRNA. Translation: CAA33607.1.
M26215 Genomic DNA. Translation: AAA02888.2.
M26216 Genomic DNA. Translation: AAA02889.1.
J04197 mRNA. Translation: AAA79008.1.
M27886 Genomic DNA. Translation: AAA58780.1.
PIRiS11761. KIRTFB.
RefSeqiNP_036753.4. NM_012621.4. [P07953-1]
UniGeneiRn.10115.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C7ZX-ray2.60A/B252-441[»]
1C80X-ray2.20A/B252-441[»]
1C81X-ray2.50A252-441[»]
1FBTX-ray2.00A/B252-441[»]
1TIPX-ray2.20A/B252-441[»]
ProteinModelPortaliP07953.
SMRiP07953.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07953. 2 interactors.
MINTiMINT-8147404.
STRINGi10116.ENSRNOP00000035212.

PTM databases

iPTMnetiP07953.
PhosphoSitePlusiP07953.

Proteomic databases

PaxDbiP07953.
PRIDEiP07953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000033656; ENSRNOP00000035212; ENSRNOG00000000165. [P07953-1]
GeneIDi24638.
KEGGirno:24638.

Organism-specific databases

CTDi5207.
RGDi3307. Pfkfb1.

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP07953.
KOiK19028.
OMAiDYIDCDQ.
OrthoDBiEOG091G0A43.
PhylomeDBiP07953.
TreeFamiTF313541.

Enzyme and pathway databases

BRENDAi2.7.1.105. 5301.
3.1.3.46. 5301.
ReactomeiR-RNO-163358. PKA-mediated phosphorylation of key metabolic factors.
R-RNO-163767. PP2A-mediated dephosphorylation of key metabolic factors.
R-RNO-70171. Glycolysis.
R-RNO-70263. Gluconeogenesis.
SABIO-RKP07953.

Miscellaneous databases

EvolutionaryTraceiP07953.
PROiP07953.

Gene expression databases

BgeeiENSRNOG00000000165.
ExpressionAtlasiP07953. baseline and differential.
GenevisibleiP07953. 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 nameiF261_RAT
AccessioniPrimary (citable) accession number: P07953
Secondary accession number(s): P16119
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 176 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, Direct protein sequencing, 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.