F26_LITCT
ID F26_LITCT Reviewed; 470 AA.
AC Q91309; Q91310;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase;
DE Short=6PF-2-K/Fru-2,6-P2ase;
DE Short=PFK/FBPase;
DE AltName: Full=6PF-2-K/Fru-2,6-P2ase liver/muscle isozymes;
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;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LIVER AND MUSCLE).
RC TISSUE=Liver, and Muscle;
RX PubMed=7509597; DOI=10.1006/bbrc.1994.1156;
RA Sakai A., Watanabe F., Furuya E.;
RT "Cloning of cDNAs for fructose 6-phosphate 2-kinase/fructose 2,6-
RT bisphosphatase from frog skeletal muscle and liver, and their expression in
RT skeletal muscle.";
RL Biochem. Biophys. Res. Commun. 198:1099-1106(1994).
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
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 -!- 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 -!- ACTIVITY REGULATION: Phosphorylation results in inhibition of the
CC kinase activity. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Liver; Synonyms=L-type;
CC IsoId=Q91309-1; Sequence=Displayed;
CC Name=Muscle; Synonyms=M-type;
CC IsoId=Q91309-2; Sequence=VSP_004685;
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000305}.
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DR EMBL; D25223; BAA04952.1; -; mRNA.
DR EMBL; D25222; BAA04951.1; -; mRNA.
DR PIR; JC2064; JC2064.
DR AlphaFoldDB; Q91309; -.
DR SMR; Q91309; -.
DR PRIDE; Q91309; -.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Hydrolase; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Transferase.
FT CHAIN 1..470
FT /note="6-phosphofructo-2-kinase/fructose-2,6-
FT bisphosphatase"
FT /id="PRO_0000179973"
FT REGION 1..249
FT /note="6-phosphofructo-2-kinase"
FT REGION 250..470
FT /note="Fructose-2,6-bisphosphatase"
FT ACT_SITE 130
FT /evidence="ECO:0000255"
FT ACT_SITE 160
FT /evidence="ECO:0000255"
FT ACT_SITE 258
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT ACT_SITE 327
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 47..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 80
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 104
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 132
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 138
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 169..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 174
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 199
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 257
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 264
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 270
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 338
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 349..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 352
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 356
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 367
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 393..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 393
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 397
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 257
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 264
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 392
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT MOD_RES 31
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..31
FT /note="MADRLRELTQTRLQKIWIPHQCDRLQQRRGS -> MEGNYKLLEDKASRIPA
FT (in isoform Muscle)"
FT /evidence="ECO:0000303|PubMed:7509597"
FT /id="VSP_004685"
SQ SEQUENCE 470 AA; 54933 MW; 53112EF3B886D310 CRC64;
MADRLRELTQ TRLQKIWIPH QCDRLQQRRG SSIPQFTNSP TMIVMVGLPA RGKTYISKKL
TRYLNWIGTP TKVFNVGQYR RDATQSYNNY QFFRADNQEA MKIRKQCALH ALKDVHTYLS
REEGHVAVFD ATNTTRERRS VILQFAKERG YKVFFIESIC DDPDIIAENI TQVKLSSPDY
TGCDREKVLE DFLKRIDCYQ MNYEPLHDDL DSSLSYIKIF NVGSRYLVNR VQDHIQSRAV
YYLMNIHVTP RSIYLSRHGE SELNLLGRIG GDSGLSVRGK QYAHELGNFI KSQQIPDLKV
WTSHMKRTIQ TAEALHVPYE QWKALNEIDA GVCEEMTYEE IQDHFPEEFA LRDQDKYRYR
YPKGESYEDI VQRLEPVIME LERQENVLVI CHQAVMRCLL AYFLDKTAEE LPYLKCPLHT
VLKLTPVAYG CKVESIYLNI EAVNTHREKP LNVEVSRDPE EALDTVPEHF
