ID   F263_BOVIN              Reviewed;         463 AA.
AC   Q28901;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ASE brain/placenta-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;
DE   Flags: Fragment;
GN   Name=PFKFB3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95251702; PubMed=7733968; DOI=10.1006/bbrc.1995.1616;
RA   Ventura F., Ambrosio S., Bartrons R., El-Maghrabi M.R., Lange A.J.,
RA   Pilkis S.J.;
RT   "Cloning and expression of a catalytic core bovine brain 6-
RT   phosphofructo-2-kinase/fructose-2,6-bisphosphatase.";
RL   Biochem. Biophys. Res. Commun. 209:1140-1148(1995).
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       phosphoglycerate mutase family.
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DR   EMBL; S77845; AAB34145.2; ALT_INIT; mRNA.
DR   IPI; IPI00708598; -.
DR   UniGene; Bt.12314; -.
DR   HSSP; P07953; 1C80.
DR   Ensembl; ENSBTAG00000008401; Bos taurus.
DR   HOVERGEN; Q28901; -.
DR   BRENDA; 2.7.1.105; 251.
DR   BRENDA; 3.1.3.46; 251.
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   CHAIN         1   >463       6-phosphofructo-2-kinase/fructose-2,6-
FT                                biphosphatase 3.
FT                                /FTId=PRO_0000179967.
FT   NP_BIND      42     49       ATP (By similarity).
FT   REGION        1    246       6-phosphofructo-2-kinase.
FT   REGION      247   >463       Fructose-2,6-bisphosphatase.
FT   ACT_SITE    125    125       Potential.
FT   ACT_SITE    155    155       Potential.
FT   ACT_SITE    255    255       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    324    324       Potential.
FT   ACT_SITE    389    389       Proton donor (By similarity).
FT   BINDING      99     99       Fructose-6-phosphate (By similarity).
FT   BINDING     191    191       Fructose-6-phosphate (By similarity).
FT   MOD_RES     462    462       Phosphoserine; by PKA (By similarity).
FT   NON_TER     463    463
SQ   SEQUENCE   463 AA;  53584 MW;  F04FA28D1F81F325 CRC64;
     MPLELTQSRV QKIWIPVDHR PSLPRTCGPK LTNSPTVIVM VGLPARGKTY ISKKLTRYLN
     WIGVPTKVFN LGEYRRDGVK QYSSYNFFRP DNEEAMKVRK QCALAALRDV KSYLTKEGGQ
     IAVFDATNTT RERRHMILHF PKENDFKVFF IESVCDDPTV VASNIMEVKI SSPDYKDCNS
     RENAMDDFMK RINCYEASYQ PLDPDNDDRD LSLIKVIDVG QRFLVNRVQD HIQRRIVYYL
     MNIHWQPRTI YLCRHGESKH NLQGKIGGDS GLSSRGRKFA NALSKFVEEQ NLKDLKVWTS
     QLKSTIQTAE ALQLPYEQWK ALNEIDAGVC EEMTYEEIKD TYPEEYALAE ADKYYYRYPT
     GESYQDLVQR LEPVIMELER QENVLVICHQ AVCVCLLAYF LDKSAEEMPY LKCPLHAVLK
     LTPIAYGCRV ESIYLNVESV STHRERSEDA KKGPNPLMRS NSH
//