F16P1_BRANA
ID F16P1_BRANA Reviewed; 411 AA.
AC Q07204;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 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].
RX PubMed=8290637; DOI=10.1104/pp.103.4.1453;
RA Rodriguez-Suarez R.J., Wolosiuk R.A.;
RT "Sequence of a cDNA encoding chloroplast fructose-1,6-bisphosphatase from
RT rapeseed.";
RL Plant Physiol. 103:1453-1454(1993).
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 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; L15303; AAB88708.1; -; mRNA.
DR PIR; T07987; T07987.
DR RefSeq; NP_001302992.1; NM_001316063.1.
DR RefSeq; XP_013717954.1; XM_013862500.1.
DR AlphaFoldDB; Q07204; -.
DR SMR; Q07204; -.
DR EnsemblPlants; CDY13182; CDY13182; GSBRNA2T00071053001.
DR GeneID; 106421663; -.
DR Gramene; CDY13182; CDY13182; GSBRNA2T00071053001.
DR KEGG; bna:106421663; -.
DR OMA; AYNARYI; -.
DR UniPathway; UPA00116; -.
DR GO; GO:0009570; C:chloroplast stroma; 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 2: Evidence at transcript level;
KW Calvin cycle; Carbohydrate metabolism; Chloroplast; Disulfide bond;
KW Hydrolase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 54..411
FT /note="Fructose-1,6-bisphosphatase, chloroplastic"
FT /id="PRO_0000008815"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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 186..189
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT DISULFID 227..232
FT /note="Redox-active (light-modulated)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 411 AA; 44446 MW; 83AC46D39EA7CECF CRC64;
MAATAGATPS SHLLLSSSRH VAASPQPRIL FPSLSGKRVA VGKNHHATGV RCMAVAADAT
AETKPAAKKK SGYELQTLTS WLLRQEMKGE IDTELTIVMS SIAMACKQIA SLVQRAGISN
LTGVQGAVNI QGEDQKKLDV VSNEVFSNCL RSSGRTGIIA SEEEDVPVAV EESYSGNYVV
VFDPLDGSSN IDAAVSTGSI FGIYSPNDEC LPDSDDTSAL GSEEERCIVN VCQPGNNLLA
AGYCMYSSSV IFVLTLGKGV FAFTLDPMYG EFVLTQENIE IPKAGKIYSF NEGNYQMWDE
NLKKYIDDLK DPGPSGKPYS ARYIGSLVGD FHRTLLYGGI YGYPRDAKSK NGKLRLLYEC
APMSFIVEQA GGKGSDGHHR VLDIQPTEIH QRVPLYIGSK EEVEKLEKYL A
