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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791Fructose 6-phosphateBy similarity
Binding sitei103 – 1031Fructose 6-phosphateBy similarity
Active sitei129 – 1291Sequence analysis
Binding sitei131 – 1311Fructose 6-phosphateBy similarity
Binding sitei137 – 1371Fructose 6-phosphateBy similarity
Active sitei159 – 1591Sequence analysis
Binding sitei173 – 1731Fructose 6-phosphateBy similarity
Binding sitei194 – 1941Fructose 6-phosphateBy similarity
Binding sitei198 – 1981Fructose 6-phosphateBy similarity
Binding sitei257 – 2571Fructose 2,6-bisphosphateBy similarity
Sitei257 – 2571Transition state stabilizerBy similarity
Active sitei258 – 2581Tele-phosphohistidine intermediateBy similarity
Binding sitei264 – 2641Fructose 2,6-bisphosphateBy similarity
Sitei264 – 2641Transition state stabilizerBy similarity
Binding sitei270 – 2701Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
Active sitei327 – 3271Proton donor/acceptorBy similarity
Binding sitei338 – 3381Fructose 2,6-bisphosphateBy similarity
Binding sitei352 – 3521Fructose 2,6-bisphosphateBy similarity
Binding sitei356 – 3561Fructose 2,6-bisphosphateBy similarity
Binding sitei367 – 3671Fructose 2,6-bisphosphateBy similarity
Sitei392 – 3921Transition state stabilizerBy similarity
Binding sitei393 – 3931Fructose 2,6-bisphosphateBy similarity
Binding sitei397 – 3971Fructose 2,6-bisphosphateBy similarity
Binding sitei429 – 4291ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 549ATPBy similarity
Nucleotide bindingi168 – 1736ATPBy similarity
Nucleotide bindingi349 – 3524ATPBy similarity
Nucleotide bindingi393 – 3975ATPBy 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.
ReactomeiR-BTA-70171. Glycolysis.
SABIO-RKP26285.

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 5315306-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2PRO_0000179963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei467 – 4671Phosphoserine; by PKA1 Publication
Modified residuei469 – 4691PhosphothreonineBy similarity
Modified residuei476 – 4761Phosphothreonine; by AMPK and PKC1 Publication
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei494 – 4941PhosphoserineBy similarity

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

ExpressionAtlasiP26285. baseline and differential.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi160003. 2 interactions.
STRINGi9913.ENSBTAP00000002753.

Structurei

3D structure databases

ProteinModelPortaliP26285.
SMRiP26285. Positions 37-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2492486-phosphofructo-2-kinaseAdd
BLAST
Regioni250 – 531282Fructose-2,6-bisphosphataseAdd
BLAST

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.
OrthoDBiEOG7M3J03.
TreeFamiTF313541.

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.

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.
SMRiP26285. Positions 37-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi160003. 2 interactions.
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.
OrthoDBiEOG7M3J03.
TreeFamiTF313541.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi20806542.

Gene expression databases

ExpressionAtlasiP26285. baseline and differential.

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. "Bovine heart fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase: complete amino acid sequence and localization of phosphorylation sites."
    Sakata J., Uyeda K.
    Proc. Natl. Acad. Sci. U.S.A. 87:4951-4955(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Bovine heart fructose 6-P,2-kinase:fructose 2,6-bisphosphatase mRNA and gene structure."
    Tsuchiya Y., Uyeda K.
    Arch. Biochem. Biophys. 310:467-474(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  3. "Phosphorylation of myocardial fructose-6-phosphate,2-kinase: fructose-2,6-bisphosphatase by cAMP-dependent protein kinase and protein kinase C. Activation by phosphorylation and amino acid sequences of the phosphorylation sites."
    Kitamura K., Kangawa K., Matsuo H., Uyeda K.
    J. Biol. Chem. 263:16796-16801(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 464-480, PHOSPHORYLATION AT SER-467 AND THR-476.
    Tissue: Heart.
  4. "Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Identification of fructose 6-phosphate binding site."
    Kitamura K., Uyeda K., Hartman F.C., Kangawa K., Matsuo H.
    J. Biol. Chem. 264:6344-6348(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 104-112; 189-204 AND 416-432.

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: May 11, 2016
This is version 132 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.