ID   F16P2_BETVU             Reviewed;         341 AA.
AC   Q42649; Q9FUA5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Fructose-1,6-bisphosphatase, cytosolic;
DE            Short=FBPase;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Amaranthaceae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Harn C.H., Daie J.;
RT   "Cloning and nucleotide sequence of a cDNA encoding the cytosolic
RT   fructose-1,6-bisphosphatases of sugarbeet (Beta Vulgaris L.).";
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16668715;
RA   Harn C.H., Daie J.;
RT   "Cloning and nucleotide sequence of a complementary DNA encoding the
RT   cytosolic fructose-1,6-bisphosphatase of sugar beet (Beta vulgaris
RT   L.).";
RL   Plant Physiol. 98:790-791(1992).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA32915.1; Type=Frameshift; Positions=8;
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DR   EMBL; M80597; AAA32915.1; ALT_SEQ; mRNA.
DR   EMBL; AF317553; AAG31813.1; -; mRNA.
DR   HSSP; P46275; 1DBZ.
DR   BRENDA; 3.1.3.11; 124.
DR   GO; GO:0005737; C:cytoplasm; 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:0005975; P:carbohydrate metabolic process; 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   Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium;
KW   Metal-binding.
FT   CHAIN         1    341       Fructose-1,6-bisphosphatase, cytosolic.
FT                                /FTId=PRO_0000200513.
FT   REGION      124    127       Substrate binding (By similarity).
FT   METAL        71     71       Magnesium 1 (By similarity).
FT   METAL       100    100       Magnesium 1 (By similarity).
FT   METAL       100    100       Magnesium 2 (By similarity).
FT   METAL       121    121       Magnesium 2 (By similarity).
FT   METAL       121    121       Magnesium 3 (By similarity).
FT   METAL       123    123       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       124    124       Magnesium 3 (By similarity).
FT   METAL       283    283       Magnesium 3 (By similarity).
FT   BINDING     215    215       Substrate (By similarity).
FT   BINDING     247    247       Substrate (By similarity).
FT   BINDING     267    267       Substrate (By similarity).
FT   BINDING     277    277       Substrate (By similarity).
SQ   SEQUENCE   341 AA;  37247 MW;  7DCC6D68B7D3FC87 CRC64;
     MDHAADATRT DLMTITRFVL NEQSKRPESR GDFTILMSHI VLGCKFVCSA VNKAGLAKLI
     GLAGETNIQG EEQKKLDVLS NEVFIKALIS SGRTCILVSE EDEEATFVEP SLRGKYCVVF
     DPLDGCSNID CGVSIGTIFG IYMVKDLNNA TLDDVLQPGK NMVAAGYCMY GSSCTLVMST
     GSGVNGFTHD PSLGEFILTH PDIKIPKKGK IYSVNEGNAK NWDGPTTKYV EKCKFPKDGS
     SPKSLRYIGS MVADVHRTLL YGGIFMYPGD KKSPNGKLRV LYEVFPMSFL MEQAGGQAFT
     GEQRALDLVP KNIHDRSPVF LGSYDDVEDI KALYAAEQKN A
//