ID   F16P1_SOYBN             Reviewed;         402 AA.
AC   Q42796;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Fructose-1,6-bisphosphatase, chloroplastic;
DE            Short=FBPase;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
DE   Flags: Precursor;
GN   Name=FBP;
OS   Glycine max (Soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Glycine.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Jinhung; TISSUE=Leaf;
RX   MEDLINE=98233132; PubMed=9571641;
RA   Jeon Y.H., Bhoo S.H., Hahn T.R.;
RT   "Molecular characterization of a cDNA encoding chloroplastic fructose-
RT   1,6-bisphosphatase from soybean (Glycine max L.).";
RL   Mol. Cells 8:113-116(1998).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- INDUCTION: Light activation through pH changes, Mg(2+) levels and
CC       also by light-modulated reduction of essential disulfide groups
CC       via the ferredoxin-thioredoxin f system (By similarity).
CC   -!- MISCELLANEOUS: In plants there are two FBPase isozymes: one in the
CC       cytosol and the other in the chloroplast.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
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DR   EMBL; L34841; AAA33956.1; -; mRNA.
DR   PIR; T07134; T07134.
DR   UniGene; Gma.33674; -.
DR   HSSP; P46275; 1DBZ.
DR   SMR; Q42796; 67-402.
DR   BRENDA; 3.1.3.11; 299.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase act...; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR000146; Fructose_bisphosphatase.
DR   InterPro; IPR017955; IMPase/FBPase.
DR   PANTHER; PTHR11556; In_FB_phphtase; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   PRINTS; PR00115; FBPHPHTASE.
DR   PRINTS; PR00377; INFBPHPHTASE.
DR   ProDom; PD001491; In_FB_phphtase; 1.
DR   PROSITE; PS00124; FBPASE; FALSE_NEG.
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     50       Chloroplast (Potential).
FT   CHAIN        51    402       Fructose-1,6-bisphosphatase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000008819.
FT   REGION      180    183       Substrate binding (By similarity).
FT   METAL       127    127       Magnesium 1 (By similarity).
FT   METAL       156    156       Magnesium 1 (By similarity).
FT   METAL       156    156       Magnesium 2 (By similarity).
FT   METAL       177    177       Magnesium 2 (By similarity).
FT   METAL       177    177       Magnesium 3 (By similarity).
FT   METAL       179    179       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       180    180       Magnesium 3 (By similarity).
FT   METAL       353    353       Magnesium 3 (By similarity).
FT   BINDING     285    285       Substrate (By similarity).
FT   BINDING     317    317       Substrate (By similarity).
FT   BINDING     335    335       Substrate (By similarity).
FT   BINDING     337    337       Substrate (By similarity).
FT   BINDING     347    347       Substrate (By similarity).
FT   DISULFID    221    226       Redox-active (light-modulated) (By
FT                                similarity).
SQ   SEQUENCE   402 AA;  43897 MW;  2EC4876454C59A3B CRC64;
     MAAATASTQL IFSKPCSPSR LCPFQLCVFD TKQVLSSGRR RHVGGSGVRC MAVGEAATTG
     TKKRSGYELQ TLTSWLLKQE QAGVIDAELT IVLSSISMAC KQIASLVQRA NISNLTGVQG
     AVNVQGEDQK KLDVVSNEVF SNCLRSSGRT GIIASEEEDV PVAVEESYSG NYIVVFDPLD
     GSSNIDAAAS TGSNFWIYSP NDECLADIDD DPTLDTTEQR CIVNVCQPGS NLLAAGYCMY
     SSSIIFVLTL GNGVFVFTLD PMYGEFVLTQ ENLQIPRAGK IYAFNEGNYQ LWDEKLKKYI
     DDLKDPGQSG KPYSARYIGS LVGDFHRTLL YGGIYGYPRD KKSKNGKLRL LYECAPINFI
     VEQAGGKGTD GLQVLRLQGT EIHQRVPLYI GEEVEKVEKY LA
//