F16P2_ORYSJ
ID F16P2_ORYSJ Reviewed; 339 AA.
AC Q0JHF8; A0A0P0VAT7; A7J2C2; O64421; Q5N9E2; Q94JN1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Fructose-1,6-bisphosphatase, cytosolic {ECO:0000305};
DE Short=FBPase {ECO:0000305};
DE EC=3.1.3.11 {ECO:0000269|Ref.8};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase {ECO:0000305};
DE AltName: Full=Protein MONOCULM 2 {ECO:0000305};
GN Name=CFBP1 {ECO:0000312|EMBL:ABI94362.1};
GN Synonyms=FBP1 {ECO:0000303|Ref.8}, MOC2 {ECO:0000303|Ref.8};
GN OrderedLocusNames=Os01g0866400 {ECO:0000312|EMBL:BAS75386.1},
GN LOC_Os01g64660 {ECO:0000305};
GN ORFNames=P0505D12.36 {ECO:0000312|EMBL:BAD81916.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RA Takahashi S., Hirose T., Imaizumi N., Ohsugi R.;
RT "Cloning of a cDNA encoding cytosolic fructose-1,6-bisphosphatase from rice
RT (Oryza sativa L.).";
RL (er) Plant Gene Register PGR98-084(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nakdong;
RA Lee S.-K., Hahn T.-R., Jeon J.-S.;
RT "Cloning and characterization of cytosolic fructose-1,6-bisphosphatase in
RT rice.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX DOI=10.5511/plantbiotechnology.12.1210a;
RA Koumoto T., Shimada H., Kusano H., She K.-C., Iwamoto M., Takano M.;
RT "Rice monoculm mutation moc2, which inhibits outgrowth of the second
RT tillers, is ascribed to lack of a fructose-1,6-bisphosphatase.";
RL Plant Biotechnol. 30:47-56(2013).
CC -!- FUNCTION: Catalyzes the first irreversible reaction from fructose-1,6-
CC bisphosphate to fructose-6-phosphate and inorganic phosphate and plays
CC an important regulatory role in sucrose biosynthesis and metabolism.
CC Required for sucrose supply and tiller bud outgrowth.
CC {ECO:0000269|Ref.8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000269|Ref.8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00636};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P00636};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00636}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Reduced tiller numbers, pale-green leaves,
CC reduced growth rate and dwarf phenotype. {ECO:0000269|Ref.8}.
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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF06820.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS75386.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB007193; BAA25422.1; -; mRNA.
DR EMBL; DQ865190; ABI94362.1; -; mRNA.
DR EMBL; AP003270; BAD81916.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06820.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; BAS75386.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK070516; BAG92000.1; -; mRNA.
DR EMBL; AK119536; BAG99676.1; -; mRNA.
DR RefSeq; XP_015641461.1; XM_015785975.1.
DR AlphaFoldDB; Q0JHF8; -.
DR SMR; Q0JHF8; -.
DR STRING; 4530.OS01T0866400-01; -.
DR PRIDE; Q0JHF8; -.
DR GeneID; 4325071; -.
DR KEGG; osa:4325071; -.
DR eggNOG; KOG1458; Eukaryota.
DR HOGENOM; CLU_039977_1_0_1; -.
DR InParanoid; Q0JHF8; -.
DR OrthoDB; 1381522at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q0JHF8; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR PROSITE; PS00124; FBPASE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..339
FT /note="Fructose-1,6-bisphosphatase, cytosolic"
FT /id="PRO_0000200517"
FT BINDING 19..23
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 30..34
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 115..116
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 124..127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 215..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 246..251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 277..279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00636"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00636"
SQ SEQUENCE 339 AA; 37035 MW; C87583E7132E8AF3 CRC64;
MDHEADAYRT DLMTITRYVL NEQSRNPEAR GDLTILLSHI VLGCKFVASA VNKAGLAKLI
GLAGETNVQG EEQKKLDVLS NEVFVKALVS SGRTCVLVSE EDEEATFVDP ALRGKYCVCF
DPLDGSSNID CGVSIGTIFG IYMIKDKENV TLEDVLQPGK NMVAAGYCMY GSSCTLVLST
GNGVNGFTLD PSLGEFILTH PDIKIPKKGK IYSVNEGNAK NWDEPTAKFV EKCKFPKDGS
SPKSLRYIGS MVADVHRTLL YGGVFLYPAD KKSPNGKLRV LYEVFPMSFL MEQAGGQSFT
GKERALDLVP TKIHERSPIF LGSFEDVEEI KGLYAAQAK
