TIGRB_DANRE
ID TIGRB_DANRE Reviewed; 257 AA.
AC Q7ZVE3; Q1L8M5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Fructose-2,6-bisphosphatase TIGAR B {ECO:0000305};
DE EC=3.1.3.46 {ECO:0000250|UniProtKB:Q9NQ88};
DE AltName: Full=TP53-induced glycolysis and apoptosis regulator B {ECO:0000250|UniProtKB:Q9NQ88};
GN Name=tigarb {ECO:0000250|UniProtKB:Q9NQ88};
GN ORFNames=si:ch211-240j22.3, zgc:56074;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=19015259; DOI=10.1074/jbc.m807821200;
RA Li H., Jogl G.;
RT "Structural and biochemical studies of TIGAR (TP53-induced glycolysis and
RT apoptosis regulator).";
RL J. Biol. Chem. 284:1748-1754(2009).
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; CR751235; CAK04686.1; -; Genomic_DNA.
DR EMBL; BC045897; AAH45897.1; -; mRNA.
DR RefSeq; NP_956485.1; NM_200191.1.
DR PDB; 3E9C; X-ray; 2.00 A; A/B=1-257.
DR PDB; 3E9D; X-ray; 2.00 A; A/B=1-257.
DR PDB; 3E9E; X-ray; 2.10 A; A/B=1-257.
DR PDBsum; 3E9C; -.
DR PDBsum; 3E9D; -.
DR PDBsum; 3E9E; -.
DR AlphaFoldDB; Q7ZVE3; -.
DR SMR; Q7ZVE3; -.
DR STRING; 7955.ENSDARP00000067391; -.
DR PaxDb; Q7ZVE3; -.
DR PRIDE; Q7ZVE3; -.
DR GeneID; 393160; -.
DR KEGG; dre:393160; -.
DR CTD; 393160; -.
DR ZFIN; ZDB-GENE-040426-885; tigarb.
DR eggNOG; KOG0235; Eukaryota.
DR InParanoid; Q7ZVE3; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; Q7ZVE3; -.
DR TreeFam; TF329053; -.
DR EvolutionaryTrace; Q7ZVE3; -.
DR PRO; PR:Q7ZVE3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; IDA:UniProtKB.
DR GO; GO:0003824; F:catalytic activity; IDA:ZFIN.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IDA: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 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Autophagy; Cytoplasm; Hydrolase; Mitochondrion;
KW Nucleus; Reference proteome.
FT CHAIN 1..257
FT /note="Fructose-2,6-bisphosphatase TIGAR B"
FT /id="PRO_0000363068"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:19015259"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:19015259"
FT SITE 183
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:19015259"
FT CONFLICT 44
FT /note="R -> H (in Ref. 1; CAK04686)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="S -> A (in Ref. 1; CAK04686)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="M -> K (in Ref. 1; CAK04686)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="L -> F (in Ref. 2; AAH45897)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="A -> V (in Ref. 2; AAH45897)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="I -> V (in Ref. 1; CAK04686)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:3E9C"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:3E9D"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3E9E"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:3E9C"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3E9C"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3E9C"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:3E9C"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3E9C"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3E9C"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3E9D"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:3E9D"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3E9D"
FT HELIX 125..147
FT /evidence="ECO:0007829|PDB:3E9C"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3E9C"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:3E9C"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3E9C"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:3E9C"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3E9C"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3E9C"
FT STRAND 220..230
FT /evidence="ECO:0007829|PDB:3E9C"
FT STRAND 233..246
FT /evidence="ECO:0007829|PDB:3E9C"
SQ SEQUENCE 257 AA; 28439 MW; 93689C4A254F9209 CRC64;
MLTFALTIVR HGETQYNRDK LLQGQGIDTP LSDTGHQQAA AAGRYLKDLH FTNVFVSNLQ
RAIQTAEIIL GNNLHSSATE MILDPLLRER GFGVAEGRPK EHLKNMANAA GQSCRDYTPP
GGETLEQVKT RFKMFLKSLF QRMLEEHGSA LSSAPSEADQ PVIAGLADDG AQNVPVHALM
VSHGAFIRIS VRHLVEDLQC CLPAGLKMNQ VFSPCPNTGI SRFIFTIHRE ESVLRATRIQ
GVFINRKDHL EEVKNSD
