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Protein

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

Gene

PFKFB1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Fructose 6-phosphateBy similarity
Binding sitei105 – 1051Fructose 6-phosphateBy similarity
Active sitei131 – 1311Sequence analysis
Binding sitei133 – 1331Fructose 6-phosphateBy similarity
Binding sitei139 – 1391Fructose 6-phosphateBy similarity
Active sitei161 – 1611Sequence analysis
Binding sitei175 – 1751Fructose 6-phosphateBy similarity
Binding sitei196 – 1961Fructose 6-phosphateBy similarity
Binding sitei200 – 2001Fructose 6-phosphateBy similarity
Binding sitei258 – 2581Fructose 2,6-bisphosphateBy similarity
Active sitei259 – 2591Tele-phosphohistidine intermediateBy similarity
Binding sitei265 – 2651Fructose 2,6-bisphosphateBy similarity
Binding sitei271 – 2711Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
Binding sitei308 – 3081Fructose 2,6-bisphosphateBy similarity
Active sitei328 – 3281Proton donor/acceptorBy similarity
Binding sitei339 – 3391Fructose 2,6-bisphosphateBy similarity
Binding sitei353 – 3531Fructose 2,6-bisphosphateBy similarity
Binding sitei357 – 3571Fructose 2,6-bisphosphateBy similarity
Binding sitei368 – 3681Fructose 2,6-bisphosphateBy similarity
Sitei393 – 3931Transition state stabilizerBy similarity
Binding sitei394 – 3941Fructose 2,6-bisphosphateBy similarity
Binding sitei398 – 3981Fructose 2,6-bisphosphateBy similarity
Binding sitei430 – 4301ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 579ATPBy similarity
Nucleotide bindingi170 – 1756ATPBy similarity
Nucleotide bindingi350 – 3534ATPBy similarity
Nucleotide bindingi394 – 3985ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.3.46. 908.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 4714706-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1PRO_0000179959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei33 – 331Phosphoserine; by PKABy similarity
Modified residuei141 – 1411PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP49872.
PRIDEiP49872.

Expressioni

Tissue specificityi

Liver.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000198.

Structurei

3D structure databases

ProteinModelPortaliP49872.
SMRiP49872. Positions 7-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2502496-phosphofructo-2-kinaseAdd
BLAST
Regioni251 – 471221Fructose-2,6-bisphosphataseAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP49872.
KOiK19028.

Family and domain databases

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.

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

P49872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQEMGELTQ TRLQKIWIPH NNGNSRLQRR RGSSIPQFTN SPTMVIMVGL
60 70 80 90 100
PARGKTYIST KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME
110 120 130 140 150
ALLIRKQCAL AALKDVHSYL SHEEGRVAVF DATNTTRERR SLILQFAKEH
160 170 180 190 200
GYKVFFIESI CNDPDVIAEN IRQVKLGSPD YIDCDREKVL EDFLKRIECY
210 220 230 240 250
EVNYQPLDDE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT VYYLMNIHVT
260 270 280 290 300
PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IQSQGISSLK
310 320 330 340 350
VGTSHMKRTI QTAEALGLPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF
360 370 380 390 400
ALRDQDKYRY RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL
410 420 430 440 450
LAYFLDKSSD ELPYLKCPLH TVLKLTPVAY GCKVESIYLN VEAVNTHREK
460 470
PENVDITREP EEALDTVPAH Y
Length:471
Mass (Da):54,657
Last modified:October 1, 1996 - v1
Checksum:i79C330B873B2D9EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64323 mRNA. Translation: AAA30696.1.
S55569 mRNA. Translation: AAB19845.1.
PIRiA44872.
RefSeqiNP_776997.3. NM_174572.4.
UniGeneiBt.562.

Genome annotation databases

GeneIDi282304.
KEGGibta:282304.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64323 mRNA. Translation: AAA30696.1.
S55569 mRNA. Translation: AAB19845.1.
PIRiA44872.
RefSeqiNP_776997.3. NM_174572.4.
UniGeneiBt.562.

3D structure databases

ProteinModelPortaliP49872.
SMRiP49872. Positions 7-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000198.

Proteomic databases

PaxDbiP49872.
PRIDEiP49872.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282304.
KEGGibta:282304.

Organism-specific databases

CTDi5207.

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP49872.
KOiK19028.

Enzyme and pathway databases

BRENDAi3.1.3.46. 908.

Miscellaneous databases

NextBioi20806103.

Family and domain databases

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...

Publicationsi

  1. "Isolation of bovine liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase cDNA: bovine liver and heart forms of the enzyme are separate gene products."
    Lange A.J., El-Maghrabi M.R., Pilkis S.J.
    Arch. Biochem. Biophys. 290:258-263(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiF261_BOVIN
AccessioniPrimary (citable) accession number: P49872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 20, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. 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.