F16P1_PEA
ID F16P1_PEA Reviewed; 407 AA.
AC P46275; Q37263;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 110.
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 Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Giant; TISSUE=Leaf;
RX PubMed=7870839; DOI=10.1104/pp.107.1.313;
RA Dong S.M., Rhim J.H., Hahn T.R.;
RT "Nucleotide sequence analysis of a cDNA encoding chloroplastic fructose-
RT 1,6-bisphosphatase from pea (Pisum sativum l.).";
RL Plant Physiol. 107:313-314(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-407.
RC STRAIN=cv. Lincoln; TISSUE=Leaf;
RX PubMed=7764999; DOI=10.1007/bf02411553;
RA Carrasco J.L., Chueca A., Prado F.E., Hermoso R., Lazaro J.J., Ramos J.L.,
RA Sahrawy M., Lopez Gorge J.;
RT "Cloning, structure and expression of a pea cDNA clone coding for a
RT photosynthetic fructose-1,6-bisphosphatase with some features different
RT from those of the leaf chloroplast enzyme.";
RL Planta 193:494-501(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 51-407.
RX PubMed=10581254; DOI=10.1093/emboj/18.23.6809;
RA Chiadmi M., Navaza A., Miginiac-Maslow M., Jacquot J.-P., Cherfils J.;
RT "Redox signalling in the chloroplast: structure of oxidized pea fructose-
RT 1,6-bisphosphate phosphatase.";
RL EMBO J. 18:6809-6815(1999).
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.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
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; L34806; AAD10213.1; -; mRNA.
DR EMBL; X68826; CAA48719.1; -; mRNA.
DR PIR; S29560; S29560.
DR PIR; T06408; T06408.
DR PDB; 1D9Q; X-ray; 2.40 A; A/B/C/D=51-407.
DR PDB; 1DBZ; X-ray; 2.65 A; A/B/C/D=51-407.
DR PDB; 1DCU; X-ray; 2.20 A; A/B/C/D=51-407.
DR PDBsum; 1D9Q; -.
DR PDBsum; 1DBZ; -.
DR PDBsum; 1DCU; -.
DR AlphaFoldDB; P46275; -.
DR SMR; P46275; -.
DR PRIDE; P46275; -.
DR BRENDA; 3.1.3.11; 4872.
DR SABIO-RK; P46275; -.
DR UniPathway; UPA00116; -.
DR EvolutionaryTrace; P46275; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0010319; C:stromule; IEA:EnsemblPlants.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:EnsemblPlants.
DR GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IEA:EnsemblPlants.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:EnsemblPlants.
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 1: Evidence at protein level;
KW 3D-structure; Calvin cycle; Carbohydrate metabolism; Chloroplast;
KW Disulfide bond; Hydrolase; Magnesium; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT CHAIN 51..407
FT /note="Fructose-1,6-bisphosphatase, chloroplastic"
FT /id="PRO_0000008817"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179..182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
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 203..223
FT CONFLICT 82
FT /note="G -> P (in Ref. 2; CAA48719)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="A -> P (in Ref. 2; CAA48719)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="A -> I (in Ref. 2; CAA48719)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="E -> K (in Ref. 2; CAA48719)"
FT /evidence="ECO:0000305"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:1DCU"
FT HELIX 86..112
FT /evidence="ECO:0007829|PDB:1DCU"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1D9Q"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:1DCU"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1D9Q"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1DCU"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1DCU"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:1DCU"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 233..254
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1DCU"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1DCU"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:1DCU"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1D9Q"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1DCU"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:1DCU"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:1DCU"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1DCU"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:1DCU"
FT HELIX 396..406
FT /evidence="ECO:0007829|PDB:1DCU"
SQ SEQUENCE 407 AA; 44511 MW; B60E9164F1F6FE9D CRC64;
MAAATASSQL IFSKPYSPSR LCPFQLCVFD AKSVLSSSRR KHVNGSGVRC MAVKEATSET
KKRSGYEIIT LTSWLLQQEQ KGIIDAELTI VLSSISMACK QIASLVQRAN ISNLTGTQGA
VNIQGEDQKK LDVISNEVFS NCLRSSGRTG IIASEEEDVA VAVEESYSGN YIVVFDPLDG
SSNLDAAVST GSIFGIYSPN DECLPDFGDD SDDNTLGTEE QRCIVNVCQP GSNLLAAGYC
MYSSSVAFVL TIGKGVFVFT LDPLYGEFVL TQENLQIPKS GEIYSFNEGN YKLWDENLKK
YIDDLKEPGP SGKPYSARYI GSLVGDFHRT LLYGGIYGYP RDKKSKNGKL RLLYECAPMS
FIVEQAGGKG SDGHQRVLDI QPTEIHQRVP LYIGSTEEVE KVEKYLA
