F16P1_WHEAT
ID F16P1_WHEAT Reviewed; 409 AA.
AC P09195;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Fructose-1,6-bisphosphatase, chloroplastic;
DE Short=FBPase;
DE EC=3.1.3.11;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
DE Flags: Precursor;
GN Name=FBP;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY LIGHT.
RC STRAIN=cv. Mardler;
RX PubMed=2843806; DOI=10.1093/nar/16.16.7931;
RA Raines C.A., Lloyd J.C., Longstaff M., Bradley D., Dyer T.A.;
RT "Chloroplast fructose-1,6-bisphosphatase: the product of a mosaic gene.";
RL Nucleic Acids Res. 16:7931-7942(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Chinese Spring; TISSUE=Etiolated shoot;
RX PubMed=1848650; DOI=10.1007/bf00269850;
RA Lloyd J.C., Raines C.A., John U.P., Dyer T.A.;
RT "The chloroplast FBPase gene of wheat: structure and expression of the
RT promoter in photosynthetic and meristematic cells of transgenic tobacco
RT plants.";
RL Mol. Gen. Genet. 225:209-216(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: In photosynthetically active tissues, and in the
CC shoot and root apical meristems. {ECO:0000269|PubMed:1848650}.
CC -!- INDUCTION: Light activation through pH changes, Mg(2+) levels and also
CC by light-modulated reduction of essential disulfide groups via the
CC ferredoxin-thioredoxin f system. {ECO:0000250}.
CC -!- MISCELLANEOUS: In plants there are two FBPase isozymes: one in the
CC cytosol and the other in the chloroplast.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; X07780; CAA30612.1; -; mRNA.
DR EMBL; X53957; CAA37908.1; -; Genomic_DNA.
DR PIR; S14060; PAWTF.
DR AlphaFoldDB; P09195; -.
DR SMR; P09195; -.
DR STRING; 4565.Traes_4AS_91D4C5213.1; -.
DR PRIDE; P09195; -.
DR EnsemblPlants; TraesCAD_scaffold_021128_01G000100.1; TraesCAD_scaffold_021128_01G000100.1; TraesCAD_scaffold_021128_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_017775_01G000300.1; TraesCLE_scaffold_017775_01G000300.1; TraesCLE_scaffold_017775_01G000300.
DR EnsemblPlants; TraesCS4A02G093100.1; TraesCS4A02G093100.1; TraesCS4A02G093100.
DR EnsemblPlants; TraesPAR_scaffold_020749_01G000300.1; TraesPAR_scaffold_020749_01G000300.1; TraesPAR_scaffold_020749_01G000300.
DR EnsemblPlants; TraesROB_scaffold_126890_01G000100.1; TraesROB_scaffold_126890_01G000100.1; TraesROB_scaffold_126890_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_059257_01G000200.1; TraesWEE_scaffold_059257_01G000200.1; TraesWEE_scaffold_059257_01G000200.
DR Gramene; TraesCAD_scaffold_021128_01G000100.1; TraesCAD_scaffold_021128_01G000100.1; TraesCAD_scaffold_021128_01G000100.
DR Gramene; TraesCLE_scaffold_017775_01G000300.1; TraesCLE_scaffold_017775_01G000300.1; TraesCLE_scaffold_017775_01G000300.
DR Gramene; TraesCS4A02G093100.1; TraesCS4A02G093100.1; TraesCS4A02G093100.
DR Gramene; TraesPAR_scaffold_020749_01G000300.1; TraesPAR_scaffold_020749_01G000300.1; TraesPAR_scaffold_020749_01G000300.
DR Gramene; TraesROB_scaffold_126890_01G000100.1; TraesROB_scaffold_126890_01G000100.1; TraesROB_scaffold_126890_01G000100.
DR Gramene; TraesWEE_scaffold_059257_01G000200.1; TraesWEE_scaffold_059257_01G000200.1; TraesWEE_scaffold_059257_01G000200.
DR eggNOG; KOG1458; Eukaryota.
DR HOGENOM; CLU_039977_1_0_1; -.
DR OMA; CMAVASE; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000019116; Unplaced.
DR Genevisible; P09195; TA.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR PROSITE; PS00124; FBPASE; 1.
PE 2: Evidence at transcript level;
KW Calvin cycle; Carbohydrate metabolism; Chloroplast; Disulfide bond;
KW Hydrolase; Magnesium; Metal-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..409
FT /note="Fructose-1,6-bisphosphatase, chloroplastic"
FT /id="PRO_0000008820"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 184..187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT DISULFID 223..228
FT /note="Redox-active (light-modulated)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 44218 MW; 607ECCC0B5E66745 CRC64;
MAAATTTTSR PLLLSRQQAA ASSLQCRLPR RPGSSLFAGQ GQASTPNVRC MAVVDTASAP
APAAARKRSS YDMITLTTWL LKQEQEGVID NEMTIVLSSI STACKQIASL VQRAPISNLT
GVQGATNVQG EDQKKLDVIS NEVFSNCLRW SGRTGVIASE EEDVPVAVEE SYSGNYIVVF
DPLDGSSNID AAVSTGSIFG IYSPSDECHI GDDATLDEVT QMCIVNVCQP GSNLLAAGYC
MYSSSVIFVL TIGTGVYVFT LDPMYGEFVL TQEKVQIPKS GKIYSFNEGN YALWDDKLKK
YMDSLKEPGT SGKPYSARYI GSLVGDFHRT MLYGGIYGYP SDQKSKNGKL RLLYECAPMS
FIAEQAGGKG SDGHQRVLDI MPTAVHQRVP LYVGSVEEVE KVEKFLSSE
