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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (6PF-2-K/Fru-2,6-P2ase 3) (PFK/FBPase 3) (6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (Fragment)

 F263_BOVIN              Reviewed;         463 AA.
Q28901;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
30-AUG-2017, entry version 114.
RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3;
Short=6PF-2-K/Fru-2,6-P2ase 3;
Short=PFK/FBPase 3;
AltName: Full=6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme;
Includes:
RecName: Full=6-phosphofructo-2-kinase;
EC=2.7.1.105;
Includes:
RecName: Full=Fructose-2,6-bisphosphatase;
EC=3.1.3.46;
Flags: Fragment;
Name=PFKFB3;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7733968; DOI=10.1006/bbrc.1995.1616;
Ventura F., Ambrosio S., Bartrons R., El-Maghrabi M.R., Lange A.J.,
Pilkis S.J.;
"Cloning and expression of a catalytic core bovine brain 6-
phosphofructo-2-kinase/fructose-2,6-bisphosphatase.";
Biochem. Biophys. Res. Commun. 209:1140-1148(1995).
-!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
-!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D-
fructose 6-phosphate + phosphate.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-
fructose 2,6-bisphosphate.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Brain.
-!- PTM: Phosphorylation by AMPK stimulates activity. {ECO:0000250}.
-!- SIMILARITY: In the C-terminal section; belongs to the
phosphoglycerate mutase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB34145.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; S77845; AAB34145.2; ALT_INIT; mRNA.
UniGene; Bt.12314; -.
ProteinModelPortal; Q28901; -.
SMR; Q28901; -.
STRING; 9913.ENSBTAP00000048148; -.
PaxDb; Q28901; -.
PRIDE; Q28901; -.
eggNOG; KOG0234; Eukaryota.
eggNOG; COG0406; LUCA.
HOGENOM; HOG000181112; -.
HOVERGEN; HBG005628; -.
InParanoid; Q28901; -.
BRENDA; 3.1.3.46; 908.
Proteomes; UP000009136; Unplaced.
GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
CDD; cd07067; HP_PGM_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR003094; 6Pfruct_kin.
InterPro; IPR013079; 6Phosfructo_kin.
InterPro; IPR013078; His_Pase_superF_clade-1.
InterPro; IPR029033; His_PPase_superfam.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001345; PG/BPGM_mutase_AS.
PANTHER; PTHR10606; PTHR10606; 1.
Pfam; PF01591; 6PF2K; 1.
Pfam; PF00300; His_Phos_1; 1.
PRINTS; PR00991; 6PFRUCTKNASE.
SMART; SM00855; PGAM; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53254; SSF53254; 1.
PROSITE; PS00175; PG_MUTASE; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Hydrolase; Kinase;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 >463 6-phosphofructo-2-kinase/fructose-2,6-
bisphosphatase 3.
/FTId=PRO_0000179967.
NP_BIND 42 50 ATP. {ECO:0000250|UniProtKB:Q16875}.
NP_BIND 164 169 ATP. {ECO:0000250|UniProtKB:Q16875}.
NP_BIND 346 349 ATP. {ECO:0000250|UniProtKB:P07953}.
NP_BIND 390 394 ATP. {ECO:0000250|UniProtKB:P07953}.
REGION 1 246 6-phosphofructo-2-kinase.
REGION 247 >463 Fructose-2,6-bisphosphatase.
ACT_SITE 125 125 {ECO:0000255}.
ACT_SITE 155 155 {ECO:0000255}.
ACT_SITE 255 255 Tele-phosphohistidine intermediate.
{ECO:0000250|UniProtKB:Q16875}.
ACT_SITE 324 324 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 75 75 Fructose 6-phosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 99 99 Fructose 6-phosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 127 127 Fructose 6-phosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 133 133 Fructose 6-phosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 169 169 Fructose 6-phosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 191 191 Fructose 6-phosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 195 195 Fructose 6-phosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 254 254 Fructose 2,6-bisphosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 261 261 Fructose 2,6-bisphosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 267 267 Fructose 2,6-bisphosphate; via amide
nitrogen. {ECO:0000250|UniProtKB:Q16875}.
BINDING 335 335 Fructose 2,6-bisphosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 353 353 Fructose 2,6-bisphosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 364 364 Fructose 2,6-bisphosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 390 390 Fructose 2,6-bisphosphate.
{ECO:0000250|UniProtKB:Q16875}.
BINDING 426 426 ATP. {ECO:0000250|UniProtKB:Q16875}.
SITE 254 254 Transition state stabilizer.
{ECO:0000250|UniProtKB:Q16875}.
SITE 261 261 Transition state stabilizer.
{ECO:0000250|UniProtKB:Q16875}.
SITE 389 389 Transition state stabilizer.
{ECO:0000250|UniProtKB:Q16875}.
MOD_RES 462 462 Phosphoserine; by AMPK and PKA.
{ECO:0000250|UniProtKB:Q16875}.
NON_TER 463 463
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


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