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Reviewed, UniProtKB/Swiss-Prot Q5NVT1 (F262_PONAB)

Last modified June 16, 2009. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2
Alternative name(s):
    PFK-2/FBPase-2
    6PF-2-K/Fru-2,6-P2ASE heart-type isozyme
Including the following 2 domains:
    1- Recommended name:
            6-phosphofructo-2-kinase
              EC=2.7.1.105
    2- Recommended name:
            Fructose-2,6-bisphosphatase
              EC=3.1.3.46
Gene names
Name: PFKFB2
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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

Catalytic activity

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 regulation

Phosphorylation results in the activation of the kinase activity By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5305306-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2
PRO_0000345129

Regions

Nucleotide binding45 – 528ATP Potential
Region1 – 2482486-phosphofructo-2-kinase
Region249 – 530282Fructose-2,6-bisphosphatase

Sites

Active site1281 Potential
Active site1581 Potential
Active site2571Tele-phosphohistidine intermediate By similarity
Active site3261 Potential
Active site3911Proton donor By similarity
Binding site1021Fructose-6-phosphate By similarity
Binding site1931Fructose-6-phosphate By similarity

Amino acid modifications

Modified residue291Phosphoserine; by PKA By similarity
Modified residue4661Phosphoserine; by PKA By similarity
Modified residue4681Phosphothreonine By similarity
Modified residue4751Phosphothreonine; by PKC By similarity
Modified residue4831Phosphoserine By similarity
Modified residue4931Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NVT1-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: B279884ABFB8780E

FASTA53061,168
        10         20         30         40         50         60 
MSGASSSEQN NNSYETKPPN LRMSEKKCSW ASYMTNSPTL IVMIGLPARG KTYVSKKLTR 

        70         80         90        100        110        120 
YLNWIGVPTK VFNLGVYRRE AVKSYKSYDF FRHDNEEAMK IRKQCALVAL EDVKAYLTEE 

       130        140        150        160        170        180 
NGQIAVFDAT NTTRERRDMI LNFAEQNSFK VFFVESVCDD PDVIAANILE VKVSSPDYPE 

       190        200        210        220        230        240 
RNRENVMEDF LKRIECYKVT YRPLDPDNYD KDLSFIKVIN VGQRFLVNRV QDYIQSKIVY 

       250        260        270        280        290        300 
YLMNIHVQPR TIYLCRHGES EFSLLGKIGG DSGLSVRGKQ FAQALRKFLE EQEITDLKVW 

       310        320        330        340        350        360 
TSQLKRTIQT AESLGVPYEQ WKILNEIDAG VCEEMTYAEI EKRYPEEFAL RDQEKYLYRY 

       370        380        390        400        410        420 
PGGESYQDLV QRLEPVIMEL ERQGNVLVIS HQAVMRCLLA YFLDKGADEL PYLRCPLHTI 

       430        440        450        460        470        480 
FKLTPVAYGC KVETIKLNVE AVNTHRDKPT NNFPKNQTPV RMRRNSFTPL SSSNTIRRPR 

       490        500        510        520        530 
NYSVGSRPLK PLSPLRAQDM QEGPTSRRPK SHSGWCTVCF PPALASCPCH 

« Hide

References

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

Cross-references

Sequence databases

CR925919 mRNA. Translation: CAI29582.1.
RefSeqNP_001127057.1.
UniGenePab.12002

3D structure databases

SMRQ5NVT1. Positions 38-451.
ModBaseSearch...

Genome annotation databases

GeneID100174086.

Phylogenomic databases

HOVERGENQ5NVT1.

Family and domain databases

InterProIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR013078. PG_mutase.
[Graphical view]
PANTHERPTHR10606. 6Pfruct_kin. 1 hit.
PfamPF01591. 6PF2K. 1 hit.
PF00300. PGAM. 1 hit.
[Graphical view]
PIRSFPIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSPR00991. 6PFRUCTKNASE.
ProtoNetSearch...

Entry information

Entry nameF262_PONAB
AccessionPrimary (citable) accession number: Q5NVT1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents