F16P1_ARATH
ID F16P1_ARATH Reviewed; 417 AA.
AC P25851; Q9M398;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Fructose-1,6-bisphosphatase 1, chloroplastic {ECO:0000305};
DE Short=FBPase1 {ECO:0000305};
DE EC=3.1.3.11 {ECO:0000305};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase {ECO:0000305};
DE AltName: Full=Protein HIGH CYCLIC ELECTRON FLOW 1 {ECO:0000303|PubMed:20081115};
DE Flags: Precursor;
GN Name=CFBP1 {ECO:0000303|PubMed:25743161};
GN Synonyms=FBP {ECO:0000303|PubMed:1651131},
GN HCEF1 {ECO:0000303|PubMed:20081115}; OrderedLocusNames=At3g54050;
GN ORFNames=F24B22.10;
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 [MRNA].
RX PubMed=1651131; DOI=10.1007/bf00036829;
RA Horsnell P.R., Raines C.A.;
RT "Nucleotide sequence of a cDNA clone encoding chloroplast fructose-1,6-
RT bisphosphatase from Arabidopsis thaliana.";
RL Plant Mol. Biol. 17:185-186(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=15448173; DOI=10.1093/jxb/erh257;
RA Sahrawy M., Avila C., Chueca A., Canovas F.M., Lopez-Gorge J.;
RT "Increased sucrose level and altered nitrogen metabolism in Arabidopsis
RT thaliana transgenic plants expressing antisense chloroplastic fructose-1,6-
RT bisphosphatase.";
RL J. Exp. Bot. 55:2495-2503(2004).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ARG-361.
RX PubMed=20081115; DOI=10.1105/tpc.109.071084;
RA Livingston A.K., Cruz J.A., Kohzuma K., Dhingra A., Kramer D.M.;
RT "An Arabidopsis mutant with high cyclic electron flow around photosystem I
RT (hcef) involving the NADPH dehydrogenase complex.";
RL Plant Cell 22:221-233(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-60, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER MET-59, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
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 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 electron flow and sucrose synthesis (PubMed:15448173, PubMed:20081115).
CC Its activity is critical for normal plant development and important for
CC the regulation of a wide range of metabolic processes
CC (PubMed:25743161). {ECO:0000269|PubMed:15448173,
CC ECO:0000269|PubMed:20081115, ECO:0000269|PubMed:25743161,
CC ECO:0000305|PubMed:15448173}.
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:0000305};
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. {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 -!- DISRUPTION PHENOTYPE: Reduced growth rate, dwarf phenotype and delayed
CC flowering. {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; X58148; CAA41154.1; -; mRNA.
DR EMBL; AL132957; CAB70979.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79179.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79180.1; -; Genomic_DNA.
DR EMBL; AF428326; AAL16256.1; -; mRNA.
DR EMBL; AY039934; AAK64038.1; -; mRNA.
DR EMBL; AY150450; AAN12891.1; -; mRNA.
DR EMBL; BT000743; AAN31884.1; -; mRNA.
DR PIR; S16582; S16582.
DR PIR; T47564; T47564.
DR RefSeq; NP_001190083.1; NM_001203154.1.
DR RefSeq; NP_190973.1; NM_115265.5.
DR AlphaFoldDB; P25851; -.
DR SMR; P25851; -.
DR BioGRID; 9889; 3.
DR IntAct; P25851; 1.
DR STRING; 3702.AT3G54050.1; -.
DR iPTMnet; P25851; -.
DR PaxDb; P25851; -.
DR PRIDE; P25851; -.
DR ProteomicsDB; 222255; -.
DR EnsemblPlants; AT3G54050.1; AT3G54050.1; AT3G54050.
DR EnsemblPlants; AT3G54050.2; AT3G54050.2; AT3G54050.
DR GeneID; 824572; -.
DR Gramene; AT3G54050.1; AT3G54050.1; AT3G54050.
DR Gramene; AT3G54050.2; AT3G54050.2; AT3G54050.
DR KEGG; ath:AT3G54050; -.
DR Araport; AT3G54050; -.
DR TAIR; locus:2080225; AT3G54050.
DR eggNOG; KOG1458; Eukaryota.
DR HOGENOM; CLU_039977_2_2_1; -.
DR InParanoid; P25851; -.
DR OMA; NDEWIFD; -.
DR OrthoDB; 1381522at2759; -.
DR PhylomeDB; P25851; -.
DR BioCyc; ARA:AT3G54050-MON; -.
DR BioCyc; MetaCyc:AT3G54050-WS-MON; -.
DR UniPathway; UPA00116; -.
DR PRO; PR:P25851; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P25851; baseline and differential.
DR Genevisible; P25851; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0010319; C:stromule; IDA:TAIR.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IMP: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:0009773; P:photosynthetic electron transport in photosystem I; IMP:TAIR.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR GO; GO:0005985; P:sucrose metabolic 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 Acetylation; Calvin cycle; Carbohydrate metabolism; Chloroplast;
KW Disulfide bond; Hydrolase; Magnesium; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255, ECO:0007744|PubMed:22223895"
FT CHAIN 60..417
FT /note="Fructose-1,6-bisphosphatase 1, chloroplastic"
FT /id="PRO_0000008814"
FT REGION 24..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191..194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 233..238
FT /note="Redox-active (light-modulated)"
FT /evidence="ECO:0000250"
FT MUTAGEN 361
FT /note="R->K: In hcef1; reduced growth rate, dwarf phenotype
FT and delayed flowering."
FT /evidence="ECO:0000269|PubMed:20081115"
FT CONFLICT 4
FT /note="T -> S (in Ref. 1; CAA41154)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="A -> S (in Ref. 1; CAA41154)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="V -> I (in Ref. 1; CAA41154)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 45162 MW; CEB17F65468746D7 CRC64;
MAATAATTTS SHLLLSSSRH VASSSQPSIL SPRSLFSNNG KRAPTGVRNH QYASGVRCMA
VAADAAETKT AARKKSGYEL QTLTGWLLRQ EMKGEIDAEL TIVMSSISLA CKQIASLVQR
AGISNLTGVQ GAVNIQGEDQ KKLDVISNEV FSNCLRSSGR TGIIASEEED VPVAVEESYS
GNYVVVFDPL DGSSNIDAAV STGSIFGIYS PNDECIVDDS DDISALGSEE QRCIVNVCQP
GNNLLAAGYC MYSSSVIFVL TLGKGVFSFT LDPMYGEFVL TQENIEIPKA GRIYSFNEGN
YQMWDDKLKK YIDDLKDPGP TGKPYSARYI GSLVGDFHRT LLYGGIYGYP RDAKSKNGKL
RLLYECAPMS FIVEQAGGKG SDGHSRVLDI QPTEIHQRVP LYIGSTEEVE KLEKYLA
