ALFC1_ORYSJ
ID ALFC1_ORYSJ Reviewed; 358 AA.
AC P17784; B7SDE6; Q07077; Q0DIB5; Q6QWQ3;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Fructose-bisphosphate aldolase 1, cytoplasmic {ECO:0000305};
DE EC=4.1.2.13 {ECO:0000250|UniProtKB:Q9SJQ9};
DE AltName: Full=Cytoplasmic aldolase {ECO:0000303|PubMed:2374721};
DE Short=cALD {ECO:0000303|PubMed:2374721};
DE AltName: Full=Gravity-specific protein GSC 233 {ECO:0000303|PubMed:1363521};
GN Name=FBA1 {ECO:0000305}; Synonyms=FBA {ECO:0000303|Ref.2};
GN OrderedLocusNames=Os05g0402700 {ECO:0000312|EMBL:BAS93924.1},
GN LOC_Os05g33380 {ECO:0000305};
GN ORFNames=OSJNBa0035J16.18 {ECO:0000312|EMBL:AAT85154.1},
GN OSJNBb0006J12.6 {ECO:0000312|EMBL:AAT85207.1};
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;
RX PubMed=2374721; DOI=10.1093/nar/18.13.3991;
RA Hidaka S., Kadowaki K., Tsutsumi K., Ishikawa K.;
RT "Nucleotide sequence of the rice cytoplasmic aldolase cDNA.";
RL Nucleic Acids Res. 18:3991-3991(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Tainung 71;
RA Huang T.-C., Chuang H.-S., Yen T.-Y., Huang Y.-W., Wu M.-L.;
RT "Nucleotide sequence of fructose 1,6-bisphosphate aldolase (FBA) of Oryza
RT sativa (Tainung No.71).";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of the fructose-bisphosphate aldolase genes in rice.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RA Yoon U.H., Kim Y.H.;
RT "Structural and expression analysis of germinating seed genes in Oryza
RT sativa L.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [6]
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 [7]
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 222-358, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Callus;
RX PubMed=1363521; DOI=10.1266/jjg.67.335;
RA Kwon S., Kikuchi S., Oono K.;
RT "Molecular cloning and characterization of gravity specific cDNA in rice
RT (Oryza sativa L.) suspension callus.";
RL Jpn. J. Genet. 67:335-348(1992).
RN [11]
RP PROTEIN SEQUENCE OF 274-283.
RC STRAIN=cv. Nipponbare; TISSUE=Stem;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(2004).
RN [12]
RP FUNCTION, AND INDUCTION BY GIBBERELLIN.
RX PubMed=15821984; DOI=10.1007/s11103-004-5920-2;
RA Konishi H., Yamane H., Maeshima M., Komatsu S.;
RT "Characterization of fructose-bisphosphate aldolase regulated by
RT gibberellin in roots of rice seedling.";
RL Plant Mol. Biol. 56:839-848(2004).
CC -!- FUNCTION: Fructose-bisphosphate aldolase that plays a key role in
CC glycolysis and gluconeogenesis (By similarity). Involved in
CC gibberellin-mediated root growth. May be regulated by CDPK13.
CC Associates with vacuolar proton ATPase (V-ATPase) and may regulate the
CC V-ATPase-mediated control of root cell elongation (PubMed:15821984).
CC {ECO:0000250|UniProtKB:Q9SJQ9, ECO:0000269|PubMed:15821984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000250|UniProtKB:Q9SJQ9};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q944G9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9SJQ9}.
CC -!- TISSUE SPECIFICITY: Expressed in callus. {ECO:0000269|PubMed:1363521}.
CC -!- INDUCTION: By gravity stress (PubMed:1363521). Induced by gibberellin
CC (PubMed:15821984). {ECO:0000269|PubMed:1363521,
CC ECO:0000269|PubMed:15821984}.
CC -!- MISCELLANEOUS: Plants silencing FBA1 display reduced root length.
CC {ECO:0000269|PubMed:15821984}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB25853.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAB25853.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB25853.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAA01911.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAA01911.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA01911.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAF17408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS93924.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE63668.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X53130; CAA37290.1; -; mRNA.
DR EMBL; AY522925; AAS05825.1; -; mRNA.
DR EMBL; EU267960; ACA50482.1; -; mRNA.
DR EMBL; GQ848038; ADM86851.1; -; mRNA.
DR EMBL; AC120991; AAT85207.1; -; Genomic_DNA.
DR EMBL; AC135418; AAT85154.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; BAS93924.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000142; EEE63668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D11137; BAA01911.1; ALT_SEQ; mRNA.
DR EMBL; S56877; AAB25853.1; ALT_SEQ; mRNA.
DR PIR; JQ0543; ADRZY.
DR PIR; T04310; T04310.
DR RefSeq; XP_015639252.1; XM_015783766.1.
DR AlphaFoldDB; P17784; -.
DR SMR; P17784; -.
DR STRING; 39947.P17784; -.
DR CarbonylDB; P17784; -.
DR PaxDb; P17784; -.
DR PRIDE; P17784; -.
DR GeneID; 4338737; -.
DR KEGG; osa:4338737; -.
DR InParanoid; P17784; -.
DR OrthoDB; 799973at2759; -.
DR PlantReactome; R-OSA-1119519; Calvin cycle.
DR PlantReactome; R-OSA-1119570; Cytosolic glycolysis.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; P17784; OS.
DR GO; GO:0005737; C:cytoplasm; ISS:Gramene.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; ISS:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Reference proteome; Schiff base; Stress response.
FT CHAIN 1..358
FT /note="Fructose-bisphosphate aldolase 1, cytoplasmic"
FT /id="PRO_0000216922"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT ACT_SITE 225
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 266..268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT SITE 358
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT CONFLICT 160
FT /note="D -> H (in Ref. 1; CAA37290)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="R -> P (in Ref. 1; CAA37290)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="E -> K (in Ref. 1; CAA37290)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="L -> R (in Ref. 1; CAA37290)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="E -> A (in Ref. 1; CAA37290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38863 MW; 2C5BBE05DD1AA83E CRC64;
MSAYCGKYKD ELIKNAAYIG TPGKGILAAD ESTGTIGKRF ASINVENVEE NRRSLRELLF
CTPGALQYLS GVILFEETLY QKTKDGKPFV DVLKEGGVLP GIKVDKGTIE VAGTEKETTT
QGHDDLGKRC AKYYEAGARF AKWRAVLKIG PNEPSQLAID LNAQGLARYA IICQENGLVP
IVEPEILVDG PHDIDRCAYV SEVVLAACYK ALNEHHVLLE GTLLKPNMVT PGSDAKKVSP
EVIAEYTVRT LQRTVPAAVP AIVFLSGGQS EEEATLNLNA MNKLSTKKPW SLSFSFGRAL
QQSTLKAWSG KAENIEKARA AFLTRCKANS EATLGTYKGD AVLGEGASES LHVKDYKY
