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Protein

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

Gene

PFKFB2

Organism
Bos taurus (Bovine)
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 results in the activation of the kinase activity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei79Fructose 6-phosphateBy similarity1
Binding sitei103Fructose 6-phosphateBy similarity1
Active sitei129Sequence analysis1
Binding sitei131Fructose 6-phosphateBy similarity1
Binding sitei137Fructose 6-phosphateBy similarity1
Active sitei159Sequence analysis1
Binding sitei173Fructose 6-phosphateBy similarity1
Binding sitei194Fructose 6-phosphateBy similarity1
Binding sitei198Fructose 6-phosphateBy similarity1
Binding sitei257Fructose 2,6-bisphosphateBy similarity1
Sitei257Transition state stabilizerBy similarity1
Active sitei258Tele-phosphohistidine intermediateBy similarity1
Binding sitei264Fructose 2,6-bisphosphateBy similarity1
Sitei264Transition state stabilizerBy similarity1
Binding sitei270Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei327Proton donor/acceptorBy similarity1
Binding sitei338Fructose 2,6-bisphosphateBy similarity1
Binding sitei352Fructose 2,6-bisphosphateBy similarity1
Binding sitei356Fructose 2,6-bisphosphateBy similarity1
Binding sitei367Fructose 2,6-bisphosphateBy similarity1
Sitei392Transition state stabilizerBy similarity1
Binding sitei393Fructose 2,6-bisphosphateBy similarity1
Binding sitei397Fructose 2,6-bisphosphateBy similarity1
Binding sitei429ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 54ATPBy similarity9
Nucleotide bindingi168 – 173ATPBy similarity6
Nucleotide bindingi349 – 352ATPBy similarity4
Nucleotide bindingi393 – 397ATPBy 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.
ReactomeiR-BTA-70171. Glycolysis.
SABIO-RKP26285.
SIGNORiP26285.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
Short name:
6PF-2-K/Fru-2,6-P2ase 2
Short name:
PFK/FBPase 2
Alternative name(s):
6PF-2-K/Fru-2,6-P2ase heart-type isozyme
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:PFKFB2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 16

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001799632 – 5316-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2Add BLAST530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei467Phosphoserine; by PKA1 Publication1
Modified residuei469PhosphothreonineBy similarity1
Modified residuei476Phosphothreonine; by AMPK and PKC1 Publication1
Modified residuei484PhosphoserineBy similarity1
Modified residuei494PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation by AMPK stimulates activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP26285.
PRIDEiP26285.

PTM databases

iPTMnetiP26285.

Expressioni

Tissue specificityi

Heart.

Gene expression databases

BgeeiENSBTAG00000002126.
ExpressionAtlasiP26285. baseline and differential.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi160003. 2 interactors.
STRINGi9913.ENSBTAP00000002753.

Structurei

3D structure databases

ProteinModelPortaliP26285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 2496-phosphofructo-2-kinaseAdd BLAST248
Regioni250 – 531Fructose-2,6-bisphosphataseAdd BLAST282

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP26285.
KOiK19029.
OMAiDQNKFAY.
OrthoDBiEOG091G0A43.
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.

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

P26285-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGNPASSSE QNNNSYETKA SLRISEKKCS WASYMTNSPT LIVMIGLPAR
60 70 80 90 100
GKTYVSKKLT RYLNWIGVPT KVFNLGVYRR QAVKSYKSYD FFRHDNEEAM
110 120 130 140 150
KIRKQCALVA LKDVKAYLTE ESGQIAVFDA TNTTRERRDL ILNFAEENSF
160 170 180 190 200
KVFFVESVCD DPDVIAANIL EVKVSSPDYP ERNRENVMDD FLKRIECYKV
210 220 230 240 250
TYQPLDPDSH DKDLSFIKVI NVGQRFLVNK VQDYIQSKIV YYLMNIHVHP
260 270 280 290 300
RTIYLCRHGE SEFNLLGKIG GDSGLSVRGK QFAQALRKFL EEQEIADLKV
310 320 330 340 350
WTSQLKRTIQ TAESLGVTYE QWKILNEIDA GVCEEMTYAE IQEQYPDEFA
360 370 380 390 400
LRDEEKYLYR YPGGESYQDL VQRLEPVIME LERQGNVLVI SHQAVMRCLL
410 420 430 440 450
AYFLDKGADE LPYLRCPLHT IFKLTPVAYG CKVETIKLNV EAVNTHRDKP
460 470 480 490 500
TNNFPKSQTP VRMRRNSFTP LSSSNTIRRP RNYSVGSRPL QPLSPLRALD
510 520 530
TQEGADQPKT QAETSRAAHR LPSPAPPTSP S
Length:531
Mass (Da):60,811
Last modified:January 23, 2007 - v2
Checksum:iE5090BBFD10BC594
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34241 mRNA. Translation: AAA30523.1.
S70453 mRNA. Translation: AAB30689.2.
PIRiS44388. A31780.
RefSeqiNP_777237.3. NM_174812.4.
UniGeneiBt.3949.

Genome annotation databases

EnsembliENSBTAT00000002753; ENSBTAP00000002753; ENSBTAG00000002126.
GeneIDi287019.
KEGGibta:287019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34241 mRNA. Translation: AAA30523.1.
S70453 mRNA. Translation: AAB30689.2.
PIRiS44388. A31780.
RefSeqiNP_777237.3. NM_174812.4.
UniGeneiBt.3949.

3D structure databases

ProteinModelPortaliP26285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi160003. 2 interactors.
STRINGi9913.ENSBTAP00000002753.

PTM databases

iPTMnetiP26285.

Proteomic databases

PaxDbiP26285.
PRIDEiP26285.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000002753; ENSBTAP00000002753; ENSBTAG00000002126.
GeneIDi287019.
KEGGibta:287019.

Organism-specific databases

CTDi5208.

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiP26285.
KOiK19029.
OMAiDQNKFAY.
OrthoDBiEOG091G0A43.
TreeFamiTF313541.

Enzyme and pathway databases

BRENDAi3.1.3.46. 908.
ReactomeiR-BTA-70171. Glycolysis.
SABIO-RKP26285.
SIGNORiP26285.

Gene expression databases

BgeeiENSBTAG00000002126.
ExpressionAtlasiP26285. baseline and differential.

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 nameiF262_BOVIN
AccessioniPrimary (citable) accession number: P26285
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.