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Protein

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

Gene

PFKFB2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Synthesis and degradation of fructose 2,6-bisphosphate.By similarity

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei78Fructose 6-phosphateBy similarity1
Binding sitei102Fructose 6-phosphateBy similarity1
Active sitei128Sequence analysis1
Binding sitei130Fructose 6-phosphateBy similarity1
Binding sitei136Fructose 6-phosphateBy similarity1
Active sitei158Sequence analysis1
Binding sitei172Fructose 6-phosphateBy similarity1
Binding sitei193Fructose 6-phosphateBy similarity1
Binding sitei197Fructose 6-phosphateBy similarity1
Binding sitei256Fructose 2,6-bisphosphateBy similarity1
Sitei256Transition state stabilizerBy similarity1
Active sitei257Tele-phosphohistidine intermediateBy similarity1
Binding sitei269Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei326Proton donor/acceptorBy similarity1
Binding sitei337Fructose 2,6-bisphosphateBy similarity1
Binding sitei351Fructose 2,6-bisphosphateBy similarity1
Binding sitei355Fructose 2,6-bisphosphateBy similarity1
Binding sitei366Fructose 2,6-bisphosphateBy similarity1
Sitei391Transition state stabilizerBy similarity1
Binding sitei392Fructose 2,6-bisphosphateBy similarity1
Binding sitei396Fructose 2,6-bisphosphateBy similarity1
Binding sitei428ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi45 – 53ATPBy similarity9
Nucleotide bindingi167 – 172ATPBy similarity6
Nucleotide bindingi348 – 351ATPBy similarity4
Nucleotide bindingi392 – 396ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00003451292 – 5306-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2Add BLAST529

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei29Phosphoserine; by PKABy similarity1
Modified residuei466Phosphoserine; by AMPK and PKABy similarity1
Modified residuei468PhosphothreonineBy similarity1
Modified residuei475Phosphothreonine; by PKCBy similarity1
Modified residuei483PhosphoserineBy similarity1
Modified residuei493PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylation by AMPK stimulates activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ5NVT1.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000000288.

Structurei

3D structure databases

ProteinModelPortaliQ5NVT1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 2486-phosphofructo-2-kinaseAdd BLAST247
Regioni249 – 530Fructose-2,6-bisphosphataseAdd BLAST282

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiQ5NVT1.
KOiK19029.

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.
[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.

Sequencei

Sequence statusi: Complete.

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

Q5NVT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGASSSEQN NNSYETKPPN LRMSEKKCSW ASYMTNSPTL IVMIGLPARG
60 70 80 90 100
KTYVSKKLTR YLNWIGVPTK VFNLGVYRRE AVKSYKSYDF FRHDNEEAMK
110 120 130 140 150
IRKQCALVAL EDVKAYLTEE NGQIAVFDAT NTTRERRDMI LNFAEQNSFK
160 170 180 190 200
VFFVESVCDD PDVIAANILE VKVSSPDYPE RNRENVMEDF LKRIECYKVT
210 220 230 240 250
YRPLDPDNYD KDLSFIKVIN VGQRFLVNRV QDYIQSKIVY YLMNIHVQPR
260 270 280 290 300
TIYLCRHGES EFSLLGKIGG DSGLSVRGKQ FAQALRKFLE EQEITDLKVW
310 320 330 340 350
TSQLKRTIQT AESLGVPYEQ WKILNEIDAG VCEEMTYAEI EKRYPEEFAL
360 370 380 390 400
RDQEKYLYRY PGGESYQDLV QRLEPVIMEL ERQGNVLVIS HQAVMRCLLA
410 420 430 440 450
YFLDKGADEL PYLRCPLHTI FKLTPVAYGC KVETIKLNVE AVNTHRDKPT
460 470 480 490 500
NNFPKNQTPV RMRRNSFTPL SSSNTIRRPR NYSVGSRPLK PLSPLRAQDM
510 520 530
QEGPTSRRPK SHSGWCTVCF PPALASCPCH
Length:530
Mass (Da):61,168
Last modified:January 4, 2005 - v1
Checksum:iB279884ABFB8780E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR925919 mRNA. Translation: CAI29582.1.
RefSeqiNP_001127057.1. NM_001133585.1.
UniGeneiPab.12002.

Genome annotation databases

GeneIDi100174086.
KEGGipon:100174086.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR925919 mRNA. Translation: CAI29582.1.
RefSeqiNP_001127057.1. NM_001133585.1.
UniGeneiPab.12002.

3D structure databases

ProteinModelPortaliQ5NVT1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000000288.

Proteomic databases

PRIDEiQ5NVT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174086.
KEGGipon:100174086.

Organism-specific databases

CTDi5208.

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
HOGENOMiHOG000181112.
HOVERGENiHBG005628.
InParanoidiQ5NVT1.
KOiK19029.

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.
[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.
ProtoNetiSearch...

Entry informationi

Entry nameiF262_PONAB
AccessioniPrimary (citable) accession number: Q5NVT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: January 4, 2005
Last modified: October 5, 2016
This is version 59 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.