ID   F16P1_BRANA             Reviewed;         411 AA.
AC   Q07204;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 59.
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   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94120014; PubMed=8290637; DOI=10.1104/pp.103.4.1453;
RA   Rodriguez-Suarez R.J., Wolosiuk R.A.;
RT   "Sequence of a cDNA encoding chloroplast fructose-1,6-bisphosphatase
RT   from rapeseed.";
RL   Plant Physiol. 103:1453-1454(1993).
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 stroma.
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; L15303; AAB88708.1; -; mRNA.
DR   PIR; T07987; T07987.
DR   HSSP; P46275; 1D9Q.
DR   SMR; Q07204; 73-411.
DR   BRENDA; 3.1.3.11; 393.
DR   GO; GO:0009570; C:chloroplast stroma; 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; 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     53       Chloroplast (By similarity).
FT   CHAIN        54    411       Fructose-1,6-bisphosphatase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000008815.
FT   REGION      186    189       Substrate binding (By similarity).
FT   METAL       133    133       Magnesium 1 (By similarity).
FT   METAL       162    162       Magnesium 1 (By similarity).
FT   METAL       162    162       Magnesium 2 (By similarity).
FT   METAL       183    183       Magnesium 2 (By similarity).
FT   METAL       183    183       Magnesium 3 (By similarity).
FT   METAL       185    185       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       186    186       Magnesium 3 (By similarity).
FT   METAL       359    359       Magnesium 3 (By similarity).
FT   BINDING     291    291       Substrate (By similarity).
FT   BINDING     323    323       Substrate (By similarity).
FT   BINDING     341    341       Substrate (By similarity).
FT   BINDING     343    343       Substrate (By similarity).
FT   BINDING     353    353       Substrate (By similarity).
FT   DISULFID    227    232       Redox-active (light-modulated) (By
FT                                similarity).
SQ   SEQUENCE   411 AA;  44446 MW;  83AC46D39EA7CECF CRC64;
     MAATAGATPS SHLLLSSSRH VAASPQPRIL FPSLSGKRVA VGKNHHATGV RCMAVAADAT
     AETKPAAKKK SGYELQTLTS WLLRQEMKGE IDTELTIVMS SIAMACKQIA SLVQRAGISN
     LTGVQGAVNI QGEDQKKLDV VSNEVFSNCL RSSGRTGIIA SEEEDVPVAV EESYSGNYVV
     VFDPLDGSSN IDAAVSTGSI FGIYSPNDEC LPDSDDTSAL GSEEERCIVN VCQPGNNLLA
     AGYCMYSSSV IFVLTLGKGV FAFTLDPMYG EFVLTQENIE IPKAGKIYSF NEGNYQMWDE
     NLKKYIDDLK DPGPSGKPYS ARYIGSLVGD FHRTLLYGGI YGYPRDAKSK NGKLRLLYEC
     APMSFIVEQA GGKGSDGHHR VLDIQPTEIH QRVPLYIGSK EEVEKLEKYL A
//