F16P2_ARATH
ID F16P2_ARATH Reviewed; 341 AA.
AC Q9MA79;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Fructose-1,6-bisphosphatase, cytosolic {ECO:0000305};
DE Short=FBPase {ECO:0000305};
DE EC=3.1.3.11 {ECO:0000269|PubMed:21253566};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase {ECO:0000305};
DE AltName: Full=Protein FRUCTOSE INSENSITIVE 1 {ECO:0000303|PubMed:21253566};
GN Name=CYFBP {ECO:0000303|PubMed:25743161};
GN Synonyms=FINS1 {ECO:0000303|PubMed:21253566}; OrderedLocusNames=At1g43670;
GN ORFNames=F2J6.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION.
RX PubMed=10998187; DOI=10.1046/j.1365-313x.2000.00847.x;
RA Strand A., Zrenner R., Trevanion S., Stitt M., Gustafsson P.,
RA Gardestroem P.;
RT "Decreased expression of two key enzymes in the sucrose biosynthesis
RT pathway, cytosolic fructose-1,6-bisphosphatase and sucrose phosphate
RT synthase, has remarkably different consequences for photosynthetic carbon
RT metabolism in transgenic Arabidopsis thaliana.";
RL Plant J. 23:759-770(2000).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 126-SER-SER-127.
RX PubMed=21253566; DOI=10.1371/journal.pgen.1001263;
RA Cho Y.H., Yoo S.D.;
RT "Signaling role of fructose mediated by FINS1/FBP in Arabidopsis
RT thaliana.";
RL PLoS Genet. 7:E1001263-E1001263(2011).
RN [6]
RP FUNCTION.
RX PubMed=22297909; DOI=10.1007/s11120-012-9720-2;
RA Cho M.H., Jang A., Bhoo S.H., Jeon J.S., Hahn T.R.;
RT "Manipulation of triose phosphate/phosphate translocator and cytosolic
RT fructose-1,6-bisphosphatase, the key components in photosynthetic sucrose
RT synthesis, enhances the source capacity of transgenic Arabidopsis plants.";
RL Photosyn. Res. 111:261-268(2012).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25743161; DOI=10.1093/jxb/erv062;
RA Rojas-Gonzalez J.A., Soto-Suarez M., Garcia-Diaz A., Romero-Puertas M.C.,
RA Sandalio L.M., Merida A., Thormaehlen I., Geigenberger P., Serrato A.J.,
RA Sahrawy M.;
RT "Disruption of both chloroplastic and cytosolic FBPase genes results in a
RT dwarf phenotype and important starch and metabolite changes in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 66:2673-2689(2015).
CC -!- FUNCTION: Catalyzes the first irreversible reaction from fructose-1,6-
CC bisphosphate to fructose-6-phosphate and inorganic phosphate and plays
CC an important regulatory role in sucrose biosynthesis and metabolism
CC (Probable). Its activity is essential to regulate starch levels
CC (PubMed:25743161). Functions in fructose-mediated signaling
CC independently of its catalytic activity in sugar metabolism. May act
CC downstream of ABA2/GIN1, which is involved in abscisic acid (ABA)
CC synthesis to regulate autotrophic transition and modulate early
CC seedling establishment after seed germination (PubMed:21253566).
CC {ECO:0000269|PubMed:21253566, ECO:0000269|PubMed:25743161,
CC ECO:0000305|PubMed:10998187, ECO:0000305|PubMed:22297909}.
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|PubMed:21253566};
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 {ECO:0000269|PubMed:21253566}. Nucleus
CC {ECO:0000269|PubMed:21253566}.
CC -!- DISRUPTION PHENOTYPE: Slight decreased in growth rate.
CC {ECO:0000269|PubMed:25743161}.
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; AC009526; AAF63117.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31985.1; -; Genomic_DNA.
DR EMBL; BT000470; AAN17447.1; -; mRNA.
DR EMBL; BT008732; AAP42745.1; -; mRNA.
DR PIR; H96499; H96499.
DR RefSeq; NP_175032.1; NM_103492.5.
DR AlphaFoldDB; Q9MA79; -.
DR SMR; Q9MA79; -.
DR BioGRID; 26178; 1.
DR IntAct; Q9MA79; 1.
DR STRING; 3702.AT1G43670.1; -.
DR PaxDb; Q9MA79; -.
DR PRIDE; Q9MA79; -.
DR ProteomicsDB; 222257; -.
DR EnsemblPlants; AT1G43670.1; AT1G43670.1; AT1G43670.
DR GeneID; 840953; -.
DR Gramene; AT1G43670.1; AT1G43670.1; AT1G43670.
DR KEGG; ath:AT1G43670; -.
DR Araport; AT1G43670; -.
DR TAIR; locus:2031103; AT1G43670.
DR eggNOG; KOG1458; Eukaryota.
DR HOGENOM; CLU_039977_1_0_1; -.
DR InParanoid; Q9MA79; -.
DR OMA; YIPENCP; -.
DR OrthoDB; 1381522at2759; -.
DR PhylomeDB; Q9MA79; -.
DR BioCyc; ARA:AT1G43670-MON; -.
DR BioCyc; MetaCyc:AT1G43670-MON; -.
DR PRO; PR:Q9MA79; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MA79; baseline and differential.
DR Genevisible; Q9MA79; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:TAIR.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009750; P:response to fructose; IMP:TAIR.
DR GO; GO:0005983; P:starch catabolic process; IMP:TAIR.
DR GO; GO:0005986; P:sucrose biosynthetic process; IMP:TAIR.
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 Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..341
FT /note="Fructose-1,6-bisphosphatase, cytosolic"
FT /id="PRO_0000200512"
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"
FT MUTAGEN 126..127
FT /note="SS->AA: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21253566"
SQ SEQUENCE 341 AA; 37287 MW; 00F18CD8588DADDA CRC64;
MDHAADAHRT DLMTITRFVL NEQSKYPESR GDFTILLSHI VLGCKFVCSA VNKAGLAKLI
GLAGETNIQG EEQKKLDVLS NDVFVNALVS SGRTSVLVSE EDEEATFVEP SKRGKYCVVF
DPLDGSSNID CGVSIGTIFG IYTLDHTDEP TTADVLKPGN EMVAAGYCMY GSSCMLVLST
GTGVHGFTLD PSLGEFILTH PDIKIPNKGN IYSVNEGNAQ NWDGPTTKYV EKCKFPKDGS
PAKSLRYVGS MVADVHRTLL YGGIFLYPAD KKSPNGKLRV LYEVFPMSFL MEQAGGQAFT
GKKRALDLVP EKIHERSPIF LGSYDDVEEI KALYAEEEKK N
