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Protein

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

Gene

Pfkfb2

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

The most important regulatory mechanism of these opposing activities is by phosphorylation and dephosphorylation of the enzyme.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei81Fructose 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 sitei259Fructose 2,6-bisphosphateBy similarity1
Sitei259Transition state stabilizerBy similarity1
Active sitei260Tele-phosphohistidine intermediateBy similarity1
Binding sitei266Fructose 2,6-bisphosphateBy similarity1
Sitei266Transition state stabilizerBy similarity1
Binding sitei272Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei329Proton donor/acceptorBy similarity1
Binding sitei340Fructose 2,6-bisphosphateBy similarity1
Binding sitei354Fructose 2,6-bisphosphateBy similarity1
Binding sitei358Fructose 2,6-bisphosphateBy similarity1
Binding sitei369Fructose 2,6-bisphosphateBy similarity1
Sitei394Transition state stabilizerBy similarity1
Binding sitei395Fructose 2,6-bisphosphateBy similarity1
Binding sitei399Fructose 2,6-bisphosphateBy similarity1
Binding sitei431ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi48 – 56ATPBy similarity9
Nucleotide bindingi170 – 175ATPBy similarity6
Nucleotide bindingi351 – 354ATPBy similarity4
Nucleotide bindingi395 – 399ATPBy similarity5

GO - Molecular functioni

  • 6-phosphofructo-2-kinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • fructose-2,6-bisphosphate 2-phosphatase activity Source: CACAO
  • kinase binding Source: RGD

GO - Biological processi

  • fructose 2,6-bisphosphate metabolic process Source: RGD
  • fructose metabolic process Source: InterPro
  • glucose catabolic process Source: RGD
  • glycolytic process Source: UniProtKB
  • lactate metabolic process Source: RGD
  • positive regulation of glucokinase activity Source: RGD
  • positive regulation of insulin secretion Source: RGD
  • pyruvate metabolic process Source: RGD
  • response to glucose 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-70171. Glycolysis.
SABIO-RKQ9JJH5.

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
RH2K
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:Pfkfb2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi3309. Pfkfb2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001799662 – 5576-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2Add BLAST556

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei32Phosphoserine; by PKABy similarity1
Modified residuei469PhosphoserineCombined sources1
Modified residuei471PhosphothreonineBy similarity1
Modified residuei478Phosphothreonine; by PKCBy similarity1
Modified residuei486PhosphoserineCombined sources1
Modified residuei496PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation by AMPK stimulates activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9JJH5.
PRIDEiQ9JJH5.

PTM databases

iPTMnetiQ9JJH5.
PhosphoSitePlusiQ9JJH5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000004162.
ExpressionAtlasiQ9JJH5. baseline and differential.
GenevisibleiQ9JJH5. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

  • kinase binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005729.

Structurei

3D structure databases

ProteinModelPortaliQ9JJH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 2516-phosphofructo-2-kinaseAdd BLAST250
Regioni252 – 557Fructose-2,6-bisphosphataseAdd BLAST306

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiQ9JJH5.
KOiK19029.
OMAiDQNKFAY.
OrthoDBiEOG091G0A43.
PhylomeDBiQ9JJH5.
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q9JJH5-1) [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
MSENSTFSTE DSSSSSYKPH ASNLRRAGKK CSWASYMTNS PTLIVMIGLP
60 70 80 90 100
ARGKTYVSKK LTRYLNWIGV PTKVFNLGVY RREAVKSYKS YDFFRHDNEE
110 120 130 140 150
AMKIRKQCAL VALEDVKAYF TEESGQIAVF DATNTTRERR DMILNFAKQN
160 170 180 190 200
AFKVFFVESV CDDPDVIAAN ILEVKVSSPD YPERNRENVM EDFLKRIECY
210 220 230 240 250
KVTYQPLDPD NYDKDLSFIK VMNVGQRFLV NRVQDYIQSK IVYYLMNIHV
260 270 280 290 300
HPRTIYLCRH GESEFNLLGK IGGDSGLSLR GKQFAQALKK FLEEQEIQDL
310 320 330 340 350
KVWTSQLKRT IQTAESLGVT YEQWKILNEI DAGVCEEMTY SEIEQRYPEE
360 370 380 390 400
FALRDQEKYL YRYPGGESYQ DLVQRLEPVI MELERQGNVL VISHQAVMRC
410 420 430 440 450
LLAYFLDKGA DELPYLRCPL HIIFKLTPVA YGCKVETITL NVEAVDTHRD
460 470 480 490 500
KPTHNFPKSQ TPVRMRRNSF TPLSSSNTIR RPRNYSVGSR PLKPLSPLRA
510 520 530 540 550
LDMQEGADQP KTQVQQGSAQ ATEHLQKALE FANGHREVEN VLAKHRRPSM

ASLTLLS
Length:557
Mass (Da):64,156
Last modified:October 1, 2000 - v1
Checksum:iD5707054E416629F
GO
Isoform 1 (identifier: Q9JJH5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     515-519: QQGSA → SIPVV
     520-547: Missing.

Show »
Length:529
Mass (Da):60,916
Checksum:i013AABF875C60840
GO
Isoform 2 (identifier: Q9JJH5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     514-536: Missing.

Show »
Length:534
Mass (Da):61,653
Checksum:i88C635DE3964CD53
GO
Isoform 4 (identifier: Q9JJH5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-536: Missing.

Show »
Length:474
Mass (Da):54,823
Checksum:i1EDFF196B219764D
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004678454 – 536Missing in isoform 4. CuratedAdd BLAST83
Alternative sequenceiVSP_004676514 – 536Missing in isoform 2. CuratedAdd BLAST23
Alternative sequenceiVSP_004677515 – 519QQGSA → SIPVV in isoform 1. Curated5
Alternative sequenceiVSP_004679520 – 547Missing in isoform 1. CuratedAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67900 mRNA. Translation: AAB29678.1.
L27084 mRNA. Translation: AAA41132.1.
AB040530 mRNA. Translation: BAA96495.1.
AB040531 mRNA. Translation: BAA96496.1.
AB040532 mRNA. Translation: BAA96497.1.
AB040533 mRNA. Translation: BAA96498.1.
PIRiJC2037.
RefSeqiNP_001029136.1. NM_001033964.2. [Q9JJH5-3]
NP_001029137.1. NM_001033965.2. [Q9JJH5-1]
NP_536725.2. NM_080477.3. [Q9JJH5-4]
XP_006249768.1. XM_006249706.3.
XP_006249769.1. XM_006249707.3.
XP_006249770.1. XM_006249708.1.
XP_006249771.1. XM_006249709.3. [Q9JJH5-4]
XP_006249773.1. XM_006249711.3. [Q9JJH5-1]
UniGeneiRn.44844.

Genome annotation databases

EnsembliENSRNOT00000005729; ENSRNOP00000005729; ENSRNOG00000004162. [Q9JJH5-1]
ENSRNOT00000037679; ENSRNOP00000030819; ENSRNOG00000004162. [Q9JJH5-4]
ENSRNOT00000050354; ENSRNOP00000044506; ENSRNOG00000004162. [Q9JJH5-3]
GeneIDi24640.
KEGGirno:24640.
UCSCiRGD:3309. rat. [Q9JJH5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67900 mRNA. Translation: AAB29678.1.
L27084 mRNA. Translation: AAA41132.1.
AB040530 mRNA. Translation: BAA96495.1.
AB040531 mRNA. Translation: BAA96496.1.
AB040532 mRNA. Translation: BAA96497.1.
AB040533 mRNA. Translation: BAA96498.1.
PIRiJC2037.
RefSeqiNP_001029136.1. NM_001033964.2. [Q9JJH5-3]
NP_001029137.1. NM_001033965.2. [Q9JJH5-1]
NP_536725.2. NM_080477.3. [Q9JJH5-4]
XP_006249768.1. XM_006249706.3.
XP_006249769.1. XM_006249707.3.
XP_006249770.1. XM_006249708.1.
XP_006249771.1. XM_006249709.3. [Q9JJH5-4]
XP_006249773.1. XM_006249711.3. [Q9JJH5-1]
UniGeneiRn.44844.

3D structure databases

ProteinModelPortaliQ9JJH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005729.

PTM databases

iPTMnetiQ9JJH5.
PhosphoSitePlusiQ9JJH5.

Proteomic databases

PaxDbiQ9JJH5.
PRIDEiQ9JJH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005729; ENSRNOP00000005729; ENSRNOG00000004162. [Q9JJH5-1]
ENSRNOT00000037679; ENSRNOP00000030819; ENSRNOG00000004162. [Q9JJH5-4]
ENSRNOT00000050354; ENSRNOP00000044506; ENSRNOG00000004162. [Q9JJH5-3]
GeneIDi24640.
KEGGirno:24640.
UCSCiRGD:3309. rat. [Q9JJH5-1]

Organism-specific databases

CTDi5208.
RGDi3309. Pfkfb2.

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
GeneTreeiENSGT00390000018751.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiQ9JJH5.
KOiK19029.
OMAiDQNKFAY.
OrthoDBiEOG091G0A43.
PhylomeDBiQ9JJH5.
TreeFamiTF313541.

Enzyme and pathway databases

BRENDAi2.7.1.105. 5301.
3.1.3.46. 5301.
ReactomeiR-RNO-70171. Glycolysis.
SABIO-RKQ9JJH5.

Miscellaneous databases

PROiQ9JJH5.

Gene expression databases

BgeeiENSRNOG00000004162.
ExpressionAtlasiQ9JJH5. baseline and differential.
GenevisibleiQ9JJH5. 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 nameiF262_RAT
AccessioniPrimary (citable) accession number: Q9JJH5
Secondary accession number(s): Q64297, Q9JHL5, Q9JJH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 137 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.