S17P_WHEAT
ID S17P_WHEAT Reviewed; 393 AA.
AC P46285;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 118.
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;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chinese Spring; TISSUE=Leaf;
RX PubMed=1374332; DOI=10.1111/j.1432-1033.1992.tb16873.x;
RA Raines C.A., Lloyd J.C., Willingham N.M., Potts S., Dyer T.A.;
RT "cDNA and gene sequences of wheat chloroplast sedoheptulose-1,7-
RT bisphosphatase reveal homology with fructose-1,6-bisphosphatases.";
RL Eur. J. Biochem. 205:1053-1059(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=8392396; DOI=10.1007/bf00015979;
RA Miles A.J., Potts S.C., Willingham N.M., Raines C.A., Lloyd J.C.;
RT "A light- and developmentally-regulated DNA-binding interaction is common
RT to the upstream sequences of the wheat Calvin cycle bisphosphatase genes.";
RL Plant Mol. Biol. 22:507-516(1993).
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 -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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 4 hours of illumination.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; X65540; CAA46507.1; -; Genomic_DNA.
DR EMBL; S63737; AAD13943.1; -; Genomic_DNA.
DR PIR; S23452; S23452.
DR AlphaFoldDB; P46285; -.
DR SMR; P46285; -.
DR STRING; 4565.Traes_3B_71DAC7F5D.1; -.
DR PRIDE; P46285; -.
DR EnsemblPlants; TraesCAD_scaffold_001683_01G000100.1; TraesCAD_scaffold_001683_01G000100.1; TraesCAD_scaffold_001683_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_029103_01G000100.1; TraesCLE_scaffold_029103_01G000100.1; TraesCLE_scaffold_029103_01G000100.
DR EnsemblPlants; TraesCS3A02G367000.1; TraesCS3A02G367000.1; TraesCS3A02G367000.
DR EnsemblPlants; TraesPAR_scaffold_001903_01G000100.1; TraesPAR_scaffold_001903_01G000100.1; TraesPAR_scaffold_001903_01G000100.
DR EnsemblPlants; TraesROB_scaffold_038030_01G000100.1; TraesROB_scaffold_038030_01G000100.1; TraesROB_scaffold_038030_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_038090_01G000100.1; TraesWEE_scaffold_038090_01G000100.1; TraesWEE_scaffold_038090_01G000100.
DR Gramene; TraesCAD_scaffold_001683_01G000100.1; TraesCAD_scaffold_001683_01G000100.1; TraesCAD_scaffold_001683_01G000100.
DR Gramene; TraesCLE_scaffold_029103_01G000100.1; TraesCLE_scaffold_029103_01G000100.1; TraesCLE_scaffold_029103_01G000100.
DR Gramene; TraesCS3A02G367000.1; TraesCS3A02G367000.1; TraesCS3A02G367000.
DR Gramene; TraesPAR_scaffold_001903_01G000100.1; TraesPAR_scaffold_001903_01G000100.1; TraesPAR_scaffold_001903_01G000100.
DR Gramene; TraesROB_scaffold_038030_01G000100.1; TraesROB_scaffold_038030_01G000100.1; TraesROB_scaffold_038030_01G000100.
DR Gramene; TraesWEE_scaffold_038090_01G000100.1; TraesWEE_scaffold_038090_01G000100.1; TraesWEE_scaffold_038090_01G000100.
DR eggNOG; KOG1458; Eukaryota.
DR OMA; PKCAIGD; -.
DR SABIO-RK; P46285; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000019116; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
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..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..393
FT /note="Sedoheptulose-1,7-bisphosphatase, chloroplastic"
FT /id="PRO_0000008824"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 179..182
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT DISULFID 115..120
FT /note="Redox-active (light-modulated)"
FT /evidence="ECO:0000255"
SQ SEQUENCE 393 AA; 42061 MW; AC27B928D5C72BA4 CRC64;
METVAAAGYA HGAATRSPAC CAAMSFSQSY RPKAARPATS FYGESLRANT ARTSFPAGRQ
SKAASRAALT TRCAIGDSLE EFLTKATPDK NLIRLLICMG EAMRTIAFKV RTASCGGTAC
VNSFGDEQLA VDMLADKLLF EALEYSHVCK YACSEEVPEL QDMGGPVEGG FSVAFDPLDG
SSIVDTNFTV GTIFGVWPGD KLTGVTGGDQ VAAAMGIYGP RTTFVVALKD CPGTHEFLLL
DEGKWQHVKD TTSIGEGKMF SPGNLRATFD NPDYDKLVNY YVKEKYTLRY TGGMVPDVNQ
IIVKEKGIFT NVTSPTAKAK LRLLFEVAPL GFLIEKAGGH SSDGKQSVLD KVISVLDERT
QVAYGSKNEI IRFEETLYGS SRLAASATVG ATA
