ID   S17P_ARATH              Reviewed;         393 AA.
AC   P46283; Q940F8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 174.
DE   RecName: Full=Sedoheptulose-1,7-bisphosphatase, chloroplastic;
DE            EC=3.1.3.37;
DE   AltName: Full=SED(1,7)P2ase;
DE   AltName: Full=Sedoheptulose bisphosphatase;
DE            Short=SBPase;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g55800; ORFNames=F1I16_210;
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 [GENOMIC DNA].
RC   STRAIN=cv. C24, and cv. Landsberg erecta; TISSUE=Leaf;
RX   PubMed=7811976; DOI=10.1007/bf00040699;
RA   Willingham N.M., Lloyd J.C., Raines C.A.;
RT   "Molecular cloning of the Arabidopsis thaliana sedoheptulose-1,7-
RT   biphosphatase gene and expression studies in wheat and Arabidopsis
RT   thaliana.";
RL   Plant Mol. Biol. 26:1191-1200(1994).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-
CC         phosphate + phosphate; Xref=Rhea:RHEA:17461, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57483, ChEBI:CHEBI:58335; EC=3.1.3.37;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000305};
CC   -!- ACTIVITY REGULATION: In continuous light, by inorganic phosphate,
CC       sed7P, glycerate and ribulose 1,5-bisphosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined except root.
CC       Highest levels found in leaves and flowers.
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. In etiolated seedlings, induction
CC       occurs only after 8 hours of illumination.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR   EMBL; S74719; AAB33001.1; -; Genomic_DNA.
DR   EMBL; AL161667; CAB81605.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79443.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7044601.1; -; Genomic_DNA.
DR   EMBL; AY054669; AAK96860.1; -; mRNA.
DR   EMBL; AY128737; AAM91137.1; -; mRNA.
DR   PIR; S51838; S51838.
DR   AlphaFoldDB; P46283; -.
DR   SMR; P46283; -.
DR   BioGRID; 10062; 4.
DR   FunCoup; P46283; 1163.
DR   IntAct; P46283; 2.
DR   STRING; 3702.P46283; -.
DR   iPTMnet; P46283; -.
DR   PaxDb; 3702-P46283; -.
DR   ProMEX; P46283; -.
DR   ProteomicsDB; 226702; -.
DR   KEGG; ath:AT3G55800; -.
DR   Araport; AT3G55800; -.
DR   TAIR; AT3G55800; SBPASE.
DR   eggNOG; KOG1458; Eukaryota.
DR   HOGENOM; CLU_039977_3_1_1; -.
DR   InParanoid; P46283; -.
DR   OMA; PKCAIGD; -.
DR   PhylomeDB; P46283; -.
DR   BioCyc; ARA:AT3G55800-MONOMER; -.
DR   BRENDA; 3.1.3.37; 399.
DR   UniPathway; UPA00116; -.
DR   CD-CODE; 4299E36E; Nucleolus.
DR   PRO; PR:P46283; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0050278; F:sedoheptulose-bisphosphatase activity; IMP:TAIR.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IDA:TAIR.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; ISS:TAIR.
DR   GO; GO:0019252; P:starch biosynthetic process; IDA:TAIR.
DR   GO; GO:0005986; P:sucrose biosynthetic process; IDA:TAIR.
DR   CDD; cd00354; FBPase; 1.
DR   FunFam; 3.30.540.10:FF:000010; Sedoheptulose-1,7-bisphosphatase, chloroplastic; 1.
DR   FunFam; 3.40.190.80:FF:000008; Sedoheptulose-1,7-bisphosphatase, chloroplastic; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 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; IPR020548; Fructose_bisphosphatase_AS.
DR   InterPro; IPR023079; SBPase.
DR   PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11556:SF35; SEDOHEPTULOSE-1,7-BISPHOSPHATASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   Pfam; PF18913; FBPase_C; 1.
DR   PRINTS; PR01958; S17BPHPHTASE.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
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; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..74
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           75..393
FT                   /note="Sedoheptulose-1,7-bisphosphatase, chloroplastic"
FT                   /id="PRO_0000008821"
FT   REGION          16..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         180..183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..121
FT                   /note="Redox-active (light-modulated)"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        145
FT                   /note="Q -> R (in Ref. 5; AAM91137/AAK96860)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  42414 MW;  ED398496A7357345 CRC64;
     METSIACYSR GILPPSVSSQ RSSTLVSPPS YSTSSSFKRL KSSSIFGDSL RLAPKSQLKA
     TKAKSNGAST VTKCEIGQSL EEFLAQATPD KGLRTLLMCM GEALRTIAFK VRTASCGGTA
     CVNSFGDEQL AVDMLADKLL FEALQYSHVC KYACSEEVPE LQDMGGPVEG GFSVAFDPLD
     GSSIVDTNFT VGTIFGVWPG DKLTGITGGD QVAAAMGIYG PRTTYVLAVK GFPGTHEFLL
     LDEGKWQHVK ETTEIAEGKM FSPGNLRATF DNSEYSKLID YYVKEKYTLR YTGGMVPDVN
     QIIVKEKGIF TNVTSPTAKA KLRLLFEVAP LGLLIENAGG FSSDGHKSVL DKTIINLDDR
     TQVAYGSKNE IIRFEETLYG TSRLKNVPIG VTA
//