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UniProtKB/Swiss-Prot entry P26285

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name F262_BOVIN
Primary accession number P26285
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 75)
Name and origin of the protein
Protein name 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2
Synonyms PFK-2/FBPase-2
6PF-2-K/Fru-2,6-P2ASE heart-type isozyme
Includes 6-phosphofructo-2-kinase
     (EC 2.7.1.105)
Fructose-2,6-bisphosphatase
     (EC 3.1.3.46)
Gene name
Name: PFKFB2
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=2164212 [NCBI, ExPASy, EBI, Israel, Japan]
Sakata J., Uyeda K.;
"Bovine heart fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase: complete amino acid sequence and localization of phosphorylation sites.";
Proc. Natl. Acad. Sci. U.S.A. 87:4951-4955(1990).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
DOI=10.1006/abbi.1994.1194; PubMed=8179334 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuchiya Y., Uyeda K.;
"Bovine heart fructose 6-P,2-kinase:fructose 2,6-bisphosphatase mRNA and gene structure.";
Arch. Biochem. Biophys. 310:467-474(1994).
[3]
 PROTEIN SEQUENCE OF 464-480, AND PHOSPHORYLATION AT SER-467 AND THR-476.
TISSUE=Heart;
PubMed=2846551 [NCBI, ExPASy, EBI, Israel, Japan]
Kitamura K., Kangawa K., Matsuo H., Uyeda K.;
"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.";
J. Biol. Chem. 263:16796-16801(1988).
[4]
 PROTEIN SEQUENCE OF 104-112; 189-204 AND 416-432.
PubMed=2539378 [NCBI, ExPASy, EBI, Israel, Japan]
Kitamura K., Uyeda K., Hartman F.C., Kangawa K., Matsuo H.;
"Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase. Identification of fructose 6-phosphate binding site.";
J. Biol. Chem. 264:6344-6348(1989).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M34241; AAA30523.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S70453; AAB30689.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S44388; A31780.
RefSeq NP_777237.3; -.
UniGene Bt.3949
3D structure databases
HSSP P07953; 1C80. [HSSP ENTRY / PDB]
ModBase P26285.
Ontologies
GO
GO:0003873; Molecular function: 6-phosphofructo-2-kinase activity (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004331; Molecular function: fructose-2,6-bisphosphate 2-phosphatase activity (inferred from electronic annotation from EC).
GO:0006003; Biological process: fructose 2,6-bisphosphate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003094; 6Pfruct_kin.
IPR013079; 6Phosfructo_kin.
IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
IPR001345; PG/BPGM_mutase.
IPR013078; PG_mutase.
Graphical view of domain structure.
PANTHER PTHR10606; 6Pfruct_kin; 1.
Pfam PF01591; 6PF2K; 1.
PF00300; PGAM; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000709; 6PFK_2-Ptase; 1.
PRINTS PR00991; 6PFRUCTKNASE.
PROSITE PS00175; PG_MUTASE; 1.
BLOCKS P26285.
ProtoNet P26285.
Genome annotation databases
Ensembl ENSBTAG00000002126; Bos taurus. [Contig view]
GeneID 287019; -.
KEGG bta:287019; -.
Phylogenomic databases
HOVERGEN P26285; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Direct protein sequencing; Hydrolase; Kinase; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   531  530     6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2. PRO_0000179963
NP_BIND   46    53  8     ATP (By similarity). 
REGION   2   249  248     6-phosphofructo-2-kinase. 
REGION   250   531  282     Fructose-2,6-bisphosphatase. 
ACT_SITE   129   129        Potential. 
ACT_SITE   159   159        Potential. 
ACT_SITE   258   258        Tele-phosphohistidine intermediate. 
ACT_SITE   327   327        Potential. 
ACT_SITE   392   392        Proton donor (By similarity). 
BINDING   103   103        Fructose-6-phosphate (By similarity). 
BINDING   194   194        Fructose-6-phosphate (By similarity). 
MOD_RES   467   467        Phosphoserine; by PKA. 
MOD_RES   476   476        Phosphothreonine; by PKC. 
Sequence information
Length: 531 AA [This is the length of the unprocessed precursor] Molecular weight: 60811 Da [This is the MW of the unprocessed precursor] CRC64: E5090BBFD10BC594 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSGNPASSSE QNNNSYETKA SLRISEKKCS WASYMTNSPT LIVMIGLPAR GKTYVSKKLT 

        70         80         90        100        110        120 
RYLNWIGVPT KVFNLGVYRR QAVKSYKSYD FFRHDNEEAM KIRKQCALVA LKDVKAYLTE 

       130        140        150        160        170        180 
ESGQIAVFDA TNTTRERRDL ILNFAEENSF KVFFVESVCD DPDVIAANIL EVKVSSPDYP 

       190        200        210        220        230        240 
ERNRENVMDD FLKRIECYKV TYQPLDPDSH DKDLSFIKVI NVGQRFLVNK VQDYIQSKIV 

       250        260        270        280        290        300 
YYLMNIHVHP RTIYLCRHGE SEFNLLGKIG GDSGLSVRGK QFAQALRKFL EEQEIADLKV 

       310        320        330        340        350        360 
WTSQLKRTIQ TAESLGVTYE QWKILNEIDA GVCEEMTYAE IQEQYPDEFA LRDEEKYLYR 

       370        380        390        400        410        420 
YPGGESYQDL VQRLEPVIME LERQGNVLVI SHQAVMRCLL AYFLDKGADE LPYLRCPLHT 

       430        440        450        460        470        480 
IFKLTPVAYG CKVETIKLNV EAVNTHRDKP TNNFPKSQTP VRMRRNSFTP LSSSNTIRRP 

       490        500        510        520        530 
RNYSVGSRPL QPLSPLRALD TQEGADQPKT QAETSRAAHR LPSPAPPTSP S
P26285 in FASTA format

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