F263_BOVIN
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 03-AUG-2022, entry version 126.
DE RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3;
DE Short=6PF-2-K/Fru-2,6-P2ase 3;
DE Short=PFK/FBPase 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 {ECO:0000269|PubMed:7733968};
DE Includes:
DE RecName: Full=Fructose-2,6-bisphosphatase;
DE EC=3.1.3.46 {ECO:0000269|PubMed:7733968};
DE Flags: Fragment;
GN Name=PFKFB3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX 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-phosphofructo-2-
RT kinase/fructose-2,6-bisphosphatase.";
RL Biochem. Biophys. Res. Commun. 209:1140-1148(1995).
CC -!- FUNCTION: Catalyzes both the synthesis and degradation of fructose 2,6-
CC bisphosphate. {ECO:0000269|PubMed:7733968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46;
CC Evidence={ECO:0000269|PubMed:7733968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17290;
CC Evidence={ECO:0000305|PubMed:7733968};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579,
CC ChEBI:CHEBI:456216; EC=2.7.1.105;
CC Evidence={ECO:0000269|PubMed:7733968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15654;
CC Evidence={ECO:0000305|PubMed:7733968};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16875}.
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:7733968}.
CC -!- PTM: Phosphorylation by AMPK stimulates activity.
CC {ECO:0000250|UniProtKB:Q16875}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB34145.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S77845; AAB34145.2; ALT_INIT; mRNA.
DR AlphaFoldDB; Q28901; -.
DR SMR; Q28901; -.
DR STRING; 9913.ENSBTAP00000048148; -.
DR PaxDb; Q28901; -.
DR PRIDE; Q28901; -.
DR eggNOG; KOG0234; Eukaryota.
DR InParanoid; Q28901; -.
DR OrthoDB; 392001at2759; -.
DR BRENDA; 3.1.3.46; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR10606; PTHR10606; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Kinase; Multifunctional enzyme; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..>463
FT /note="6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
FT 3"
FT /id="PRO_0000179967"
FT REGION 1..246
FT /note="6-phosphofructo-2-kinase"
FT REGION 247..>463
FT /note="Fructose-2,6-bisphosphatase"
FT REGION 444..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /evidence="ECO:0000255"
FT ACT_SITE 155
FT /evidence="ECO:0000255"
FT ACT_SITE 255
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT ACT_SITE 324
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 75
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 99
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 127
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 133
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 164..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 169
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 191
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 195
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 254
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 261
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 267
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 335
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 346..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 353
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 364
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 390..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 390
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 254
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 261
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 389
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT MOD_RES 462
FT /note="Phosphoserine; by AMPK and PKA"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT NON_TER 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
