TIGRA_DANRE
ID TIGRA_DANRE Reviewed; 256 AA.
AC Q29RA5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Probable fructose-2,6-bisphosphatase TIGAR A {ECO:0000305};
DE EC=3.1.3.46 {ECO:0000250|UniProtKB:Q9NQ88};
DE AltName: Full=TP53-induced glycolysis and apoptosis regulator A {ECO:0000250|UniProtKB:Q9NQ88};
GN Name=tigara {ECO:0000250|UniProtKB:Q9NQ88}; ORFNames=zgc:136900;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2006) 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; BC114302; AAI14303.1; -; mRNA.
DR RefSeq; NP_001034925.1; NM_001039836.1.
DR AlphaFoldDB; Q29RA5; -.
DR SMR; Q29RA5; -.
DR STRING; 7955.ENSDARP00000097862; -.
DR PaxDb; Q29RA5; -.
DR Ensembl; ENSDART00000111158; ENSDARP00000097862; ENSDARG00000051749.
DR GeneID; 664696; -.
DR KEGG; dre:664696; -.
DR CTD; 664696; -.
DR ZFIN; ZDB-GENE-060312-25; tigara.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00940000163946; -.
DR HOGENOM; CLU_033323_16_0_1; -.
DR InParanoid; Q29RA5; -.
DR OMA; HGETQCN; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; Q29RA5; -.
DR TreeFam; TF329053; -.
DR Reactome; R-DRE-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:Q29RA5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000051749; Expressed in muscle tissue and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0004083; F:bisphosphoglycerate 2-phosphatase activity; 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 GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IBA:GO_Central.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; IBA:GO_Central.
DR GO; GO:0043456; P:regulation of pentose-phosphate shunt; IBA:GO_Central.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 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..256
FT /note="Probable fructose-2,6-bisphosphatase TIGAR A"
FT /id="PRO_0000363067"
FT REGION 147..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q7ZVE3"
SQ SEQUENCE 256 AA; 28180 MW; E87E233413A199A7 CRC64;
MLAFGLTVVR HGETQCNKDG LLQGQKIDSL LSDIGIQQSE AAGQYLRDVK FTNVFVSNMK
RAKQTAEIIV RNNRTCHDLE LVADPSLIER SFGIAEGGRV IDMKNMAKAA GQPLPEFTPP
EGETMEQVKL RIKDFLKAMY QRIANDHQDK VQDGGTSSAD ESTEAPAGLA NDGVSSVPVH
ALVVGHGAYM SIAMRYFFED LKCPVPRGLD PAQQFSICPN TGMCRFIITL KCSSVDIALS
DIKCVFINRR DHFKTN
