S17P_ARATH
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 03-AUG-2022, entry version 159.
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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S74719; AAB33001.1; -; Genomic_DNA.
DR EMBL; AL161667; CAB81605.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79443.1; -; Genomic_DNA.
DR EMBL; AY054669; AAK96860.1; -; mRNA.
DR EMBL; AY128737; AAM91137.1; -; mRNA.
DR PIR; S51838; S51838.
DR RefSeq; NP_191139.1; NM_115438.4.
DR AlphaFoldDB; P46283; -.
DR SMR; P46283; -.
DR BioGRID; 10062; 3.
DR IntAct; P46283; 2.
DR STRING; 3702.AT3G55800.1; -.
DR iPTMnet; P46283; -.
DR SWISS-2DPAGE; P46283; -.
DR World-2DPAGE; 0003:P46283; -.
DR PaxDb; P46283; -.
DR PRIDE; P46283; -.
DR ProMEX; P46283; -.
DR ProteomicsDB; 226702; -.
DR EnsemblPlants; AT3G55800.1; AT3G55800.1; AT3G55800.
DR GeneID; 824746; -.
DR Gramene; AT3G55800.1; AT3G55800.1; AT3G55800.
DR KEGG; ath:AT3G55800; -.
DR Araport; AT3G55800; -.
DR TAIR; locus:2078941; AT3G55800.
DR eggNOG; KOG1458; Eukaryota.
DR HOGENOM; CLU_039977_3_1_1; -.
DR InParanoid; P46283; -.
DR OMA; PKCAIGD; -.
DR OrthoDB; 1381522at2759; -.
DR PhylomeDB; P46283; -.
DR BioCyc; ARA:AT3G55800-MON; -.
DR BRENDA; 3.1.3.37; 399.
DR UniPathway; UPA00116; -.
DR PRO; PR:P46283; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P46283; baseline and differential.
DR Genevisible; P46283; AT.
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:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050278; F:sedoheptulose-bisphosphatase activity; IMP:TAIR.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IDA:TAIR.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
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: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 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; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PRINTS; PR01958; S17BPHPHTASE.
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. 4; 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
