ID F16P1_ARATH Reviewed; 417 AA. AC P25851; Q9M398; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 05-MAY-2009, entry version 78. 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; OrderedLocusNames=At3g54050; ORFNames=F24B22.10; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91329733; PubMed=1651131; DOI=10.1007/BF00036829; RA Horsnell P.R., Raines C.A.; RT "Nucleotide sequence of a cDNA clone encoding chloroplast fructose- RT 1,6-bisphosphatase from Arabidopsis thaliana."; RL Plant Mol. Biol. 17:185-186(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). 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. 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; X58148; CAA41154.1; -; mRNA. DR EMBL; AL132957; CAB70979.1; -; Genomic_DNA. DR EMBL; AF428326; AAL16256.1; -; mRNA. DR EMBL; AY039934; AAK64038.1; -; mRNA. DR EMBL; AY150450; AAN12891.1; -; mRNA. DR EMBL; BT000743; AAN31884.1; -; mRNA. DR IPI; IPI00530130; -. DR PIR; S16582; S16582. DR PIR; T47564; T47564. DR RefSeq; NP_190973.1; -. DR UniGene; At.22619; -. DR HSSP; P46275; 1DBZ. DR SMR; P25851; 78-417. DR PRIDE; P25851; -. DR ProMEX; P25851; -. DR GeneID; 824572; -. DR GenomeReviews; BA000014_GR; AT3G54050. DR KEGG; ath:AT3G54050; -. DR NMPDR; fig|3702.1.peg.16704; -. DR TAIR; At3g54050; -. DR OMA; P25851; IDAAVST. DR BRENDA; 3.1.3.11; 302. DR ArrayExpress; P25851; -. DR GermOnline; AT3G54050; Arabidopsis thaliana. DR GO; GO:0048046; C:apoplast; IDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR. 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 GO; GO:0009409; P:response to cold; IEP:TAIR. 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 1: Evidence at protein level; KW Calvin cycle; Carbohydrate metabolism; Chloroplast; Complete proteome; KW Disulfide bond; Hydrolase; Magnesium; Metal-binding; Plastid; KW Transit peptide. FT TRANSIT 1 59 Chloroplast (Potential). FT CHAIN 60 417 Fructose-1,6-bisphosphatase, FT chloroplastic. FT /FTId=PRO_0000008814. FT REGION 191 194 Substrate binding (By similarity). FT METAL 138 138 Magnesium 1 (By similarity). FT METAL 167 167 Magnesium 1 (By similarity). FT METAL 167 167 Magnesium 2 (By similarity). FT METAL 188 188 Magnesium 2 (By similarity). FT METAL 188 188 Magnesium 3 (By similarity). FT METAL 190 190 Magnesium 2; via carbonyl oxygen (By FT similarity). FT METAL 191 191 Magnesium 3 (By similarity). FT METAL 365 365 Magnesium 3 (By similarity). FT BINDING 297 297 Substrate (By similarity). FT BINDING 329 329 Substrate (By similarity). FT BINDING 347 347 Substrate (By similarity). FT BINDING 349 349 Substrate (By similarity). FT BINDING 359 359 Substrate (By similarity). FT DISULFID 233 238 Redox-active (light-modulated) (By FT similarity). FT CONFLICT 4 4 T -> S (in Ref. 1; CAA41154). FT CONFLICT 66 66 A -> S (in Ref. 1; CAA41154). FT CONFLICT 133 133 V -> I (in Ref. 1; CAA41154). SQ SEQUENCE 417 AA; 45162 MW; CEB17F65468746D7 CRC64; MAATAATTTS SHLLLSSSRH VASSSQPSIL SPRSLFSNNG KRAPTGVRNH QYASGVRCMA VAADAAETKT AARKKSGYEL QTLTGWLLRQ EMKGEIDAEL TIVMSSISLA CKQIASLVQR AGISNLTGVQ GAVNIQGEDQ KKLDVISNEV FSNCLRSSGR TGIIASEEED VPVAVEESYS GNYVVVFDPL DGSSNIDAAV STGSIFGIYS PNDECIVDDS DDISALGSEE QRCIVNVCQP GNNLLAAGYC MYSSSVIFVL TLGKGVFSFT LDPMYGEFVL TQENIEIPKA GRIYSFNEGN YQMWDDKLKK YIDDLKDPGP TGKPYSARYI GSLVGDFHRT LLYGGIYGYP RDAKSKNGKL RLLYECAPMS FIVEQAGGKG SDGHSRVLDI QPTEIHQRVP LYIGSTEEVE KLEKYLA //