ID   F16P2_BETVU             Reviewed;         341 AA.
AC   Q42649; Q9FUA5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Fructose-1,6-bisphosphatase, cytosolic;
DE            Short=FBPase;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Harn C.H., Daie J.;
RT   "Cloning and nucleotide sequence of a cDNA encoding the cytosolic fructose-
RT   1,6-bisphosphatases of sugarbeet (Beta Vulgaris L.).";
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16668715; DOI=10.1104/pp.98.2.790;
RA   Harn C.H., Daie J.;
RT   "Cloning and nucleotide sequence of a complementary DNA encoding the
RT   cytosolic fructose-1,6-bisphosphatase of sugar beet (Beta vulgaris L.).";
RL   Plant Physiol. 98:790-791(1992).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA32915.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M80597; AAA32915.1; ALT_SEQ; mRNA.
DR   EMBL; AF317553; AAG31813.1; -; mRNA.
DR   AlphaFoldDB; Q42649; -.
DR   SMR; Q42649; -.
DR   GO; GO:0005737; C:cytoplasm; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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   Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..341
FT                   /note="Fructose-1,6-bisphosphatase, cytosolic"
FT                   /id="PRO_0000200513"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  37247 MW;  7DCC6D68B7D3FC87 CRC64;
     MDHAADATRT DLMTITRFVL NEQSKRPESR GDFTILMSHI VLGCKFVCSA VNKAGLAKLI
     GLAGETNIQG EEQKKLDVLS NEVFIKALIS SGRTCILVSE EDEEATFVEP SLRGKYCVVF
     DPLDGCSNID CGVSIGTIFG IYMVKDLNNA TLDDVLQPGK NMVAAGYCMY GSSCTLVMST
     GSGVNGFTHD PSLGEFILTH PDIKIPKKGK IYSVNEGNAK NWDGPTTKYV EKCKFPKDGS
     SPKSLRYIGS MVADVHRTLL YGGIFMYPGD KKSPNGKLRV LYEVFPMSFL MEQAGGQAFT
     GEQRALDLVP KNIHDRSPVF LGSYDDVEDI KALYAAEQKN A