ID TIGAR_XENLA Reviewed; 275 AA.
AC Q4V7R0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Fructose-2,6-bisphosphatase TIGAR {ECO:0000305};
DE EC=3.1.3.46 {ECO:0000250|UniProtKB:Q9NQ88};
DE AltName: Full=TP53-induced glycolysis and apoptosis regulator {ECO:0000250|UniProtKB:Q9NQ88};
GN Name=tigar {ECO:0000250|UniProtKB:Q9NQ88};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate
CC as well as fructose-1,6-bisphosphate. Acts as a negative regulator of
CC glycolysis by lowering intracellular levels of fructose-2,6-
CC bisphosphate in a p53/TP53-dependent manner, resulting in the pentose
CC phosphate pathway (PPP) activation and NADPH production. Contributes to
CC the generation of reduced glutathione to cause a decrease in
CC intracellular reactive oxygen species (ROS) content, correlating with
CC its ability to protect cells from oxidative or metabolic stress-induced
CC cell death. May play a role in mitophagy inhibition.
CC {ECO:0000250|UniProtKB:Q8BZA9, ECO:0000250|UniProtKB:Q9NQ88}.
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:0000250|UniProtKB:Q9NQ88};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BZA9}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NQ88}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q8BZA9}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
CC -!- CAUTION: Not expected to have any kinase activity. {ECO:0000305}.
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DR EMBL; BC097765; AAH97765.1; -; mRNA.
DR RefSeq; NP_001089513.1; NM_001096044.1.
DR AlphaFoldDB; Q4V7R0; -.
DR SMR; Q4V7R0; -.
DR MaxQB; Q4V7R0; -.
DR DNASU; 734566; -.
DR GeneID; 734566; -.
DR KEGG; xla:734566; -.
DR AGR; Xenbase:XB-GENE-1008476; -.
DR CTD; 734566; -.
DR Xenbase; XB-GENE-1008476; tigar.S.
DR OrthoDB; 88851at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 734566; Expressed in testis and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Autophagy; Cytoplasm; Hydrolase; Mitochondrion; Nucleus;
KW Reference proteome.
FT CHAIN 1..275
FT /note="Fructose-2,6-bisphosphatase TIGAR"
FT /id="PRO_0000363069"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7ZVE3"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q7ZVE3"
FT SITE 198
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q7ZVE3"
SQ SEQUENCE 275 AA; 30658 MW; 95DF4520AEF1C924 CRC64;
MARFALTIVR HGETRYNKEK LLQGQGIDEP LSEMGFKQAD AAGRFLSNVR FTHVFSSDLI
RAKQTACAIM RNNQLSEDIK IMYDPRLRER KYGDAEGRPL SELKVMAKKA GGQCPSYTPP
GGETLEQVRA CAKDFFEYLC QLVMAESSVK EKSELGASGM VGIMSTDLAP FVNHNKEPTI
FGESRDVTLD ASVLLVSHGA YMRNWIKYFV EDLQFTFPPE LKKSRELSVS PNTGISHFIV
TVGSGATRKP EIQCVCINLH GHLSDIDADT SHYQV
//
