ID   F264_MACFA              Reviewed;         469 AA.
AC   Q4R8B6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ASE testis-type isozyme;
DE   Includes:
DE     RecName: Full=6-phosphofructo-2-kinase;
DE              EC=2.7.1.105;
DE   Includes:
DE     RecName: Full=Fructose-2,6-bisphosphatase;
DE              EC=3.1.3.46;
GN   Name=PFKFB4; ORFNames=QtsA-12874;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-
CC       fructose 2,6-bisphosphate.
CC   -!- ENZYME REGULATION: The most important regulatory mechanism of
CC       these opposing activities is by phosphorylation and
CC       dephosphorylation of the enzyme (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       phosphoglycerate mutase family.
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DR   EMBL; AB168541; BAE00656.1; -; mRNA.
DR   SMR; Q4R8B6; 38-469.
DR   HOVERGEN; Q4R8B6; -.
DR   BRENDA; 2.7.1.105; 3438.
DR   BRENDA; 3.1.3.46; 3438.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase act...; IEA:EC.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
DR   InterPro; IPR001345; PG/BPGM_mutase.
DR   InterPro; IPR013078; PG_mutase.
DR   PANTHER; PTHR10606; 6Pfruct_kin; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    469       6-phosphofructo-2-kinase/fructose-2,6-
FT                                biphosphatase 4.
FT                                /FTId=PRO_0000268186.
FT   NP_BIND      46     53       ATP (Potential).
FT   REGION        2    249       6-phosphofructo-2-kinase.
FT   REGION      250    469       Fructose-2,6-bisphosphatase.
FT   ACT_SITE    129    129       Potential.
FT   ACT_SITE    159    159       Potential.
FT   ACT_SITE    257    257       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    326    326       Potential.
FT   ACT_SITE    391    391       Proton donor (By similarity).
FT   BINDING     103    103       Fructose-6-phosphate (By similarity).
FT   BINDING     194    194       Fructose-6-phosphate (By similarity).
FT   MOD_RES     444    444       Phosphothreonine; by PKC (Potential).
SQ   SEQUENCE   469 AA;  54071 MW;  0ABB1148962456D8 CRC64;
     MASPRELTQN PLKKIWMPYS NGRPALHACQ RGVCMTNCPT LIVMVGLPAR GKTYISKKLT
     RYLNWIGVPT REFNVGQYRR NMVKTYKSFE FFLPDNEEGL KIRKQCALAA LRDVRRFLSE
     EGGHVAVFDA TNTTRERRAT IFNFGEQNGY KTFFVESICV DPEVIAANIV QVKLGSPDYV
     NRDSDEATED FMRRIECYEN SYESLDEDLD RDLSYIKIMD VGQSYVVNRV ADHIQSRIVY
     YLMNIHVTPR SIYLCRHGES ELNLKGRIGG DPGLSPRGRE FAKSLAQFIS DQNIKDLKVW
     TSQMKRTIQT AEALGVPYEQ WKVLNEIDAG VCEEMTYEEI QDNYPLEFAL RDQDKYRYRY
     PKGESYEDLV QRLEPVIMEL ERQENVLVIC HQAVMRCLLA YFLDKAAEQL PYLKCPLHTV
     LKLTPVAYGC KVESIFLNVA AVNTHRDRPQ NVDISRPPEE ALVTVPAHQ
//