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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781Fructose 6-phosphateBy similarity
Binding sitei102 – 1021Fructose 6-phosphateBy similarity
Active sitei128 – 1281Sequence analysis
Binding sitei130 – 1301Fructose 6-phosphateBy similarity
Binding sitei136 – 1361Fructose 6-phosphateBy similarity
Active sitei158 – 1581Sequence analysis
Binding sitei172 – 1721Fructose 6-phosphateBy similarity
Binding sitei193 – 1931Fructose 6-phosphateBy similarity
Binding sitei197 – 1971Fructose 6-phosphateBy similarity
Binding sitei256 – 2561Fructose 2,6-bisphosphateBy similarity
Sitei256 – 2561Transition state stabilizerBy similarity
Active sitei257 – 2571Tele-phosphohistidine intermediateBy similarity
Binding sitei269 – 2691Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
Active sitei326 – 3261Proton donor/acceptorBy similarity
Binding sitei337 – 3371Fructose 2,6-bisphosphateBy similarity
Binding sitei351 – 3511Fructose 2,6-bisphosphateBy similarity
Binding sitei355 – 3551Fructose 2,6-bisphosphateBy similarity
Binding sitei366 – 3661Fructose 2,6-bisphosphateBy similarity
Sitei391 – 3911Transition state stabilizerBy similarity
Binding sitei392 – 3921Fructose 2,6-bisphosphateBy similarity
Binding sitei396 – 3961Fructose 2,6-bisphosphateBy similarity
Binding sitei428 – 4281ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 539ATPBy similarity
Nucleotide bindingi167 – 1726ATPBy similarity
Nucleotide bindingi348 – 3514ATPBy similarity
Nucleotide bindingi392 – 3965ATPBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 5305296-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2PRO_0000345129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei29 – 291Phosphoserine; by PKABy similarity
Modified residuei466 – 4661Phosphoserine; by AMPK and PKABy similarity
Modified residuei468 – 4681PhosphothreonineBy similarity
Modified residuei475 – 4751Phosphothreonine; by PKCBy similarity
Modified residuei483 – 4831PhosphoserineBy similarity
Modified residuei493 – 4931PhosphoserineBy similarity

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.
SMRiQ5NVT1. Positions 36-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2482476-phosphofructo-2-kinaseAdd
BLAST
Regioni249 – 530282Fructose-2,6-bisphosphataseAdd
BLAST

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

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.
SMRiQ5NVT1. Positions 36-448.
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

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...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

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: January 20, 2016
This is version 56 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.