ID F16P2_SACHY Reviewed; 343 AA. AC Q43139; 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; GN Name=CFBP; OS Saccharum hybrid (Sugarcane). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Saccharum. OX NCBI_TaxID=15819; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. H65-7052; RA Grof C.P.L., Glassop D., Bugos R.C., Moore P.H.; RT "Sequence of a cDNA encoding cytosolic fructose-1,6-bisphosphatase RT from Sugarcane (Saccharum L.)."; RL (er) Plant Gene Register PGR95-057. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X89006; CAA61409.1; ALT_INIT; mRNA. DR PIR; S57717; S57717. DR HSSP; P00637; 1BK4. DR Gramene; Q43139; -. 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 1 343 Fructose-1,6-bisphosphatase, cytosolic. FT /FTId=PRO_0000200519. 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 343 AA; 37409 MW; 9C15B43B6935CDE9 CRC64; MDHAADAHRT DLMTITRHVL NEQSRNPESR GDFTILLSHI VLGCKFVASA VNKAGLAQLI GLAGETNVQG EEQKKLDVLS NEVFVKALVS SGRTCVLVSE EDEETTFVDP KLRGKYCVCF DPLDGSSNID CGVSIGTIFG IYMIKDKDNV TLSDVLQPGK DMLAAGYCMY GSSCTLVLST GTGVNGFTLD PSLGEFILTH PDIKIPKKGK IYSVNEGNAK NWDVPVAKFV EKCKYPKDGS PPKSLRYIGS MVADVHRTLL YGGVFLYPAD QKSPNGKLRV LYEVFPMSFL MEQAGGQSFT GKERALDLVP TKIHERSPIF LGSYDDVEEI KALYAEQAKS SSA //