F16P2_BRANA
ID F16P2_BRANA Reviewed; 339 AA.
AC P46267;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cotyledon;
RX PubMed=7630967; DOI=10.1104/pp.108.3.1335;
RA Laroche A., Frick M.M., Kazala C., Weselake R.J., Thomas J.E.;
RT "Isolation and characterization of an oilseed rape fructose-1,6-
RT bisphosphatase cDNA.";
RL Plant Physiol. 108:1335-1336(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 -!- 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}.
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DR EMBL; U20179; AAA82750.1; -; mRNA.
DR PIR; T07853; T07853.
DR RefSeq; NP_001302604.1; NM_001315675.1.
DR AlphaFoldDB; P46267; -.
DR SMR; P46267; -.
DR PRIDE; P46267; -.
DR GeneID; 106401056; -.
DR KEGG; bna:106401056; -.
DR BRENDA; 3.1.3.11; 944.
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..339
FT /note="Fructose-1,6-bisphosphatase, cytosolic"
FT /id="PRO_0000200514"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 37156 MW; 3844CD90F3C6DD33 CRC64;
MDHEADAFRD LMTITRFVLN EQSKYPESRG DFTILLSNIV LGCKFVCSAV NKAGLAKLIG
LAGDTNIQGE EQKKLDVLSN DVFVKALVSS GRTSVLVSEE DEEATFVESS KCGKYCVVFD
PLDGSSNIDC GVSIGTIFGI YTMEHSDEPT TKDVLKPGNE MVAAGYCMYG SSCMLVLSTG
TGVHGFTLDP SLGEFILTHP DIKIPKKGNI YSVNEGNAQN WDGPTTKYVE RCKYPKDGSP
AKSLRYVGSM VADVHRTLLY GGIFLYPADK KSPNGKLRVL YEVFPMAFLM EQAGGQAFTG
KKRALDLVPK KIHERSPIFL GSYDDVEEIK ALYAEEEKN
