F16P1_SPIOL
ID F16P1_SPIOL Reviewed; 415 AA.
AC P22418; O20251;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 116.
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;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling;
RX PubMed=8980497; DOI=10.1007/bf00019100;
RA Martin W., Mustafa A.Z., Henze K., Schnarrenberger C.;
RT "Higher-plant chloroplast and cytosolic fructose-1,6-bisphosphatase
RT isoenzymes: origins via duplication rather than prokaryote-eukaryote
RT divergence.";
RL Plant Mol. Biol. 32:485-491(1996).
RN [2]
RP PROTEIN SEQUENCE OF 58-415.
RX PubMed=2159755; DOI=10.1016/0003-9861(90)90475-e;
RA Marcus F., Harrsch P.B.;
RT "Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase.";
RL Arch. Biochem. Biophys. 279:151-157(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=7703244; DOI=10.1021/bi00013a020;
RA Villeret V., Huang S., Zhang Y., Lipscomb W.N.;
RT "Structural aspects of the allosteric inhibition of fructose-1,6-
RT bisphosphatase by AMP: the binding of both the substrate analogue 2,5-
RT anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by
RT X-ray crystallography.";
RL Biochemistry 34:4307-4315(1995).
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.
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.
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; L76555; AAD10207.1; -; mRNA.
DR PIR; T09085; T09085.
DR PDB; 1SPI; X-ray; 2.80 A; A/B/C/D=58-415.
DR PDBsum; 1SPI; -.
DR AlphaFoldDB; P22418; -.
DR SMR; P22418; -.
DR PRIDE; P22418; -.
DR OrthoDB; 1381522at2759; -.
DR BRENDA; 3.1.3.11; 5812.
DR SABIO-RK; P22418; -.
DR UniPathway; UPA00116; -.
DR EvolutionaryTrace; P22418; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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 Direct protein sequencing; Disulfide bond; Hydrolase; Magnesium;
KW Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:2159755"
FT CHAIN 58..415
FT /note="Fructose-1,6-bisphosphatase, chloroplastic"
FT /id="PRO_0000008818"
FT REGION 207..232
FT /note="Involved in light regulation"
FT /evidence="ECO:0000255"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 188..191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT DISULFID 231..236
FT /note="Redox-active (light-modulated)"
FT /evidence="ECO:0000250"
FT CONFLICT 66
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="E -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="D -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 96..116
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 239..260
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:1SPI"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1SPI"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 377..388
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:1SPI"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:1SPI"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:1SPI"
SQ SEQUENCE 415 AA; 45230 MW; A23465129F54A5A1 CRC64;
MASIGPATTT AVKLRSSIFN PQSSTLSPSQ QCITFTKSLH SFPTATRHNV ASGVRCMAAV
GEAATETKAR TRSKYEIETL TGWLLKQEMA GVIDAELTIV LSSISLACKQ IASLVQRAGI
SNLTGIQGAV NIQGEDQKKL DVVSNEVFSS CLRSSGRTGI IASEEEDVPV AVEESYSGNY
IVVFDPLDGS SNIDAAVSTG SIFGIYSPND ECIVDSDHDD ESQLSAEEQR CVVNVCQPGD
NLLAAGYCMY SSSVIFVLTI GKGVYAFTLD PMYGEFVLTS EKIQIPKAGK IYSFNEGNYK
MWDDKLKKYM DDLKEPGESQ KPYSSRYIGS LVGDFHRTLL YGGIYGYPRD AKSKNGKLRL
LYECAPMSFI VEQAGGKGSD GHQRILDIQP TEIHQRVPLY IGSVEEVEKL EKYLA