F16P1_ORYSI
ID F16P1_ORYSI Reviewed; 406 AA.
AC A2XEX2; B0LSR2;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Fructose-1,6-bisphosphatase, chloroplastic {ECO:0000305};
DE Short=FBPase {ECO:0000305};
DE EC=3.1.3.11 {ECO:0000269|Ref.2};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=OsI_10887 {ECO:0000312|EMBL:EAY89382.1},
GN OsI_10888 {ECO:0000312|EMBL:EAY89383.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-406, FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX DOI=10.1007/s11240-013-0334-y;
RA Chatterjee J., Patra B., Mukherjee R., Basak P., Mukherjee S., Ray S.,
RA Bhattacharyya S., Maitra S., Ghoshdastidar K., Ghosh S., Sengupta S.,
RA Majumder A.L.;
RT "Cloning, characterization and expression of a chloroplastic fructose-1,6-
RT bisphosphatase from Porteresia coarctata conferring salt-tolerance in
RT transgenic tobacco.";
RL Plant Cell Tissue Organ Cult. 114:395-409(2013).
CC -!- FUNCTION: Catalyzes the irreversible reaction from fructose-1,6-
CC bisphosphate to fructose-6-phosphate and inorganic phosphate, to
CC regenerate the primary CO(2) acceptor molecule, ribulose-1,5-
CC bisphosphate (Probable). Involved in the regulation of photosynthetic
CC performance and sucrose synthesis (Ref.2). {ECO:0000269|Ref.2,
CC ECO:0000305|Ref.2}.
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 Evidence={ECO:0000269|Ref.2};
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 -!- ACTIVITY REGULATION: Inhibited by sodium chloride. {ECO:0000269|Ref.2}.
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000305}.
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; CM000128; EAY89382.1; -; Genomic_DNA.
DR EMBL; CM000128; EAY89383.1; -; Genomic_DNA.
DR EMBL; EU370973; ABY75186.1; -; mRNA.
DR AlphaFoldDB; A2XEX2; -.
DR SMR; A2XEX2; -.
DR STRING; 39946.A2XEX2; -.
DR PRIDE; A2XEX2; -.
DR EnsemblPlants; BGIOSGA011042-TA; BGIOSGA011042-PA; BGIOSGA011042.
DR EnsemblPlants; BGIOSGA011043-TA; BGIOSGA011043-PA; BGIOSGA011043.
DR Gramene; BGIOSGA011042-TA; BGIOSGA011042-PA; BGIOSGA011042.
DR Gramene; BGIOSGA011043-TA; BGIOSGA011043-PA; BGIOSGA011043.
DR HOGENOM; CLU_039977_1_0_1; -.
DR OMA; AYNARYI; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000007015; Chromosome 3.
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 1: Evidence at protein level;
KW Calvin cycle; Carbohydrate metabolism; Chloroplast; Disulfide bond;
KW Hydrolase; Magnesium; Metal-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..406
FT /note="Fructose-1,6-bisphosphatase, chloroplastic"
FT /id="PRO_0000438734"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181..184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT DISULFID 222..227
FT /note="Redox-active (light-modulated)"
FT /evidence="ECO:0000250"
FT CONFLICT 343
FT /note="K -> R (in Ref. 2; ABY75186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 43604 MW; 1665BB680EC06069 CRC64;
MAAAATTSSH LLLLSRQQAA ASLQCGLSFR RQPGRLAGGS SAPSVRCMAA VDTASAPAAT
EASKKSSYEI TTLTTWLLKQ EQAGTIDGEM TIVLASISTA CKQIASLVQR APISNLTGVQ
GAVNVQGEDQ KKLDVVSNEV FSNCLKSSGR TGVIASEEED VPVAVEESYS GNYIVVFDPL
DGSSNIDAAV STGSIFGIYS PNDECLADIA DDQNLDQVEQ RCIVSVCQPG SNLLAAGYCM
YSSSVIFVLT IGTGVYVFTL DPMYGEFVLT QEKVQIPKAG KIYAFNEGNY ALWDDKLKSY
MDSLKEPGPS GKPYSARYIG SLVGDFHRTL LYGGIYGYPR DQKSKNGKLR LLYECAPMSF
IVEQAGGKGS DGHQRILDIM PTEIHQRVPL YIGSVEEVEK VEKFLA
