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 27-MAR-2024, entry version 139. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 39947-P17784; -. DR GeneID; 4338737; -. DR KEGG; osa:4338737; -. DR InParanoid; P17784; -. DR OrthoDB; 3595068at2759; -. 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 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 CDD; cd00948; FBP_aldolase_I_a; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR NCBIfam; NF033379; FrucBisAld_I; 1. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR11627:SF80; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. DR Genevisible; P17784; OS. 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 //