Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)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 intermediateBy similarity1
Binding sitei265Fructose 2,6-bisphosphateBy similarity1
Binding sitei271Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Binding sitei308Fructose 2,6-bisphosphateBy similarity1
Active sitei328Proton donor/acceptorBy similarity1
Binding sitei339Fructose 2,6-bisphosphateBy similarity1
Binding sitei353Fructose 2,6-bisphosphateBy similarity1
Binding sitei357Fructose 2,6-bisphosphateBy similarity1
Binding sitei368Fructose 2,6-bisphosphateBy similarity1
Sitei393Transition state stabilizerBy similarity1
Binding sitei394Fructose 2,6-bisphosphateBy similarity1
Binding sitei398Fructose 2,6-bisphosphateBy similarity1
Binding sitei430ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi49 – 57ATPBy similarity9
Nucleotide bindingi170 – 175ATPBy similarity6
Nucleotide bindingi350 – 353ATPBy similarity4
Nucleotide bindingi394 – 398ATPBy similarity5

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001799592 – 4716-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1Add BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei33Phosphoserine; by PKABy similarity1
Modified residuei141PhosphoserineBy similarity1

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.
ModBaseiSearch...
MobiDBiSearch...

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.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP49872.
KOiK19028.

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.

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.
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.

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_BOVIN
AccessioniPrimary (citable) accession number: P49872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 5, 2016
This is version 118 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.