S17P_CHLRE
ID S17P_CHLRE Reviewed; 389 AA.
AC P46284;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Name=CSBP;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CC-406;
RX PubMed=8165256; DOI=10.1104/pp.104.3.1101;
RA Hahn D., Kueck U.;
RT "Nucleotide sequence of a cDNA encoding the chloroplast sedoheptulose-1,7-
RT bisphosphatase from Chlamydomonas reinhardtii.";
RL Plant Physiol. 104:1101-1102(1994).
RN [2]
RP 3D-STRUCTURE MODELING OF 66-380.
RX PubMed=8811868; DOI=10.1046/j.1365-313x.1996.10030553.x;
RA Anderson L.E., Huppe H.C., Li A.D., Stevens F.J.;
RT "Identification of a potential redox-sensitive interdomain disulfide in the
RT sedoheptulose bisphosphatase of Chlamydomonas reinhardtii.";
RL Plant J. 10:553-560(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:0000305}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; X74418; CAA52439.1; -; mRNA.
DR PIR; T08128; T08128.
DR AlphaFoldDB; P46284; -.
DR SMR; P46284; -.
DR STRING; 3055.EDP04487; -.
DR ProMEX; P46284; -.
DR eggNOG; KOG1458; Eukaryota.
DR BRENDA; 3.1.3.37; 1318.
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 GO; GO:0019252; P:starch biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0005986; P:sucrose biosynthetic process; IEA:EnsemblPlants.
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 ?..389
FT /note="Sedoheptulose-1,7-bisphosphatase, chloroplastic"
FT /id="PRO_0000008822"
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 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 176..179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 323
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 389 AA; 41760 MW; 69A631982E632416 CRC64;
MAAMMMRQKV AGAIAGERRS AVAPKMGRAA TAPVVVASAN ASAFKGAAVT ARVKASTRAA
RVQSRRTAVL TQAKIGDSLA EFLVEATPDP KLRHVMMSMA EATRTIAHKV RTASCAGTAC
VNSFGDEQLA VDMVADKLLF EALKYSHVCK LACSEEVPEP VDMGGEGFCV AFDPLDGSSS
SDTNFAVGTI FGVWPGDKLT NITGREQVAA GMGIYGPRTV FCIALKDAPG CHEFLLMDDG
KWMHVKETTH IGEGKMFAPG NLRATFDNPA YERLINFYLG EKYTLRYTGG IVPDLFQIIV
KEKGVFTNLT SPTTKAKLRI LFEVAPLALL IEKAGGASSC DGKAVSALDI PILVCDQRTQ
ICYGSIGEVR RFEEYMYGTS PRFSEKVVA
