位置:首页 > 蛋白库 > S17P_SPIOL
S17P_SPIOL
ID   S17P_SPIOL              Reviewed;         387 AA.
AC   O20252;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling;
RX   PubMed=8980497; DOI=10.1007/bf00019100;
RA   Martin W., Mustafa A.Z., Henze K., Schnarrenberger C.;
RT   "Higher-plant chloroplast and cytosolic fructose-1,6-bisphosphatase
RT   isoenzymes: origins via duplication rather than prokaryote-eukaryote
RT   divergence.";
RL   Plant Mol. Biol. 32:485-491(1996).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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; L76556; AAB81104.1; -; mRNA.
DR   PIR; T09086; T09086.
DR   AlphaFoldDB; O20252; -.
DR   SMR; O20252; -.
DR   IntAct; O20252; 1.
DR   PRIDE; O20252; -.
DR   OrthoDB; 1381522at2759; -.
DR   SABIO-RK; O20252; -.
DR   UniPathway; UPA00116; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..387
FT                   /note="Sedoheptulose-1,7-bisphosphatase, chloroplastic"
FT                   /id="PRO_0000008823"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         170
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         170
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         173..176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255"
FT   BINDING         284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..114
FT                   /note="Redox-active (light-modulated)"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   387 AA;  42081 MW;  746AE554C6844B79 CRC64;
     METSMACCSR SIVLPRVSPQ HSSALVPSSI NLKSLKSSSL FGESLRMTTK SSVRVNKAKN
     SSLVTKCELG DSLEEFLAKA TTDKGLIRLM MCMGEALRTI GFKVRTASCG GTQCVNTFGD
     EQLAIDVLAD KLLFEALNYS HFCKYACSEE LPELQDMGGP VDGGFSVAFD PLDGSSIVDT
     NFSVGTIFGV WPGDKLTGVT GRDQVAAAMG IYGPRTTYVL ALKDYPGTHE FLLLDEGKWQ
     HVKETTEINE GKLFCPGNLR ATSDNADYAK LIQYYIKEKY TLRYTGGMVP DVNQIIVKEK
     GIFTNVISPT AKAKLRLLFE VAPLGFLIEK AGGHSSEGTK SVLDIEVKNL DDRTQVAYGS
     LNEIIRFEKT LYGSSRLEEP VPVGAAA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024