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UniProtKB/Swiss-Prot entry P25851


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name F16P1_ARATH
Primary accession number P25851
Secondary accession number Q9M398
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on June 6, 2002 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 72)
Name and origin of the protein
Protein name Fructose-1,6-bisphosphatase, chloroplastic [Precursor]
Synonyms FBPase
EC 3.1.3.11
D-fructose-1,6-bisphosphate 1-phosphohydrolase
Gene name
Name: FBP
OrderedLocusNames: At3g54050
ORFNames: F24B22.10
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1007/BF00036829; PubMed=1651131 [NCBI, ExPASy, EBI, Israel, Japan]
Horsnell P.R., Raines C.A.;
"Nucleotide sequence of a cDNA clone encoding chloroplast fructose-1,6-bisphosphatase from Arabidopsis thaliana.";
Plant Mol. Biol. 17:185-186(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X58148; CAA41154.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132957; CAB70979.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF428326; AAL16256.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY039934; AAK64038.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY150450; AAN12891.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000743; AAN31884.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S16582; S16582.
T47564; T47564.
RefSeq NP_190973.1; -.
UniGene At.22619
3D structure databases
HSSP P46275; 1DBZ. [HSSP ENTRY / PDB]
SMR P25851; 78-417.
ModBase P25851.
Organism-specific databases
TAIR At3g54050; -.
Gene expression databases
ArrayExpress P25851; -.
GermOnline AT3G54050; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0042132; Molecular function: fructose 1,6-bisphosphate 1-phosphatase activity (inferred from electronic annotation from EC).
GO:0019253; Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000146; In_FB_phphtase.
Graphical view of domain structure.
PANTHER PTHR11556; In_FB_phphtase; 1.
Pfam PF00316; FBPase; 1.
Pfam graphical view of domain structure.
PRINTS PR00115; FBPHPHTASE.
PR00377; INFBPHPHTASE.
ProDom PD001491; In_FB_phphtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00124; FBPASE; 1.
BLOCKS P25851.
ProtoNet P25851.
Proteomic databases
ProMEX P25851; -.
Genome annotation databases
GeneID 824572; -.
GenomeReviews BA000014_GR; AT3G54050.
KEGG ath:AT3G54050; -.
NMPDR fig|3702.1.peg.16704; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calvin cycle; Carbohydrate metabolism; Chloroplast; Complete proteome; Hydrolase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    59  59     Chloroplast (Potential). 
CHAIN   60   417  358     Fructose-1,6-bisphosphatase, chloroplastic. PRO_0000008814
ACT_SITE   359   359        By similarity. 
DISULFID   233   238        Redox-active (light-modulated) (By similarity). 
CONFLICT   4     4        T -> S (in Ref. 1; CAA41154). 
CONFLICT   66    66        A -> S (in Ref. 1; CAA41154). 
CONFLICT   133   133        V -> I (in Ref. 1; CAA41154). 
Sequence information
Length: 417 AA [This is the length of the unprocessed precursor] Molecular weight: 45162 Da [This is the MW of the unprocessed precursor] CRC64: CEB17F65468746D7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAATAATTTS SHLLLSSSRH VASSSQPSIL SPRSLFSNNG KRAPTGVRNH QYASGVRCMA 

        70         80         90        100        110        120 
VAADAAETKT AARKKSGYEL QTLTGWLLRQ EMKGEIDAEL TIVMSSISLA CKQIASLVQR 

       130        140        150        160        170        180 
AGISNLTGVQ GAVNIQGEDQ KKLDVISNEV FSNCLRSSGR TGIIASEEED VPVAVEESYS 

       190        200        210        220        230        240 
GNYVVVFDPL DGSSNIDAAV STGSIFGIYS PNDECIVDDS DDISALGSEE QRCIVNVCQP 

       250        260        270        280        290        300 
GNNLLAAGYC MYSSSVIFVL TLGKGVFSFT LDPMYGEFVL TQENIEIPKA GRIYSFNEGN 

       310        320        330        340        350        360 
YQMWDDKLKK YIDDLKDPGP TGKPYSARYI GSLVGDFHRT LLYGGIYGYP RDAKSKNGKL 

       370        380        390        400        410 
RLLYECAPMS FIVEQAGGKG SDGHSRVLDI QPTEIHQRVP LYIGSTEEVE KLEKYLA 

P25851 in FASTA format

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View entry in raw text format (no links)
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