ID ALFP2_ARATH Reviewed; 398 AA. AC Q944G9; Q5XEU6; Q9SVJ6; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 135. DE RecName: Full=Fructose-bisphosphate aldolase 2, chloroplastic {ECO:0000305}; DE Short=AtFBA2 {ECO:0000303|PubMed:22561114}; DE EC=4.1.2.13 {ECO:0000305}; DE Flags: Precursor; GN Name=FBA2 {ECO:0000303|PubMed:22561114}; OrderedLocusNames=At4g38970; GN ORFNames=F19H22.70; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [6] RP SUBCELLULAR LOCATION. RC STRAIN=cv. Col-2; RX PubMed=16414959; DOI=10.1074/jbc.m511939200; RA Vidi P.-A., Kanwischer M., Baginsky S., Austin J.R., Csucs G., Doermann P., RA Kessler F., Brehelin C.; RT "Tocopherol cyclase (VTE1) localization and vitamin E accumulation in RT chloroplast plastoglobule lipoprotein particles."; RL J. Biol. Chem. 281:11225-11234(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC STRAIN=cv. Columbia; RX PubMed=16461379; DOI=10.1104/pp.105.076083; RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.; RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A RT surprising site for differential accumulation of metabolic enzymes."; RL Plant Physiol. 140:984-997(2006). RN [8] RP PHOSPHORYLATION. RX PubMed=18768909; DOI=10.1104/pp.108.124594; RA Ghelis T., Bolbach G., Clodic G., Habricot Y., Miginiac E., Sotta B., RA Jeannette E.; RT "Protein tyrosine kinases and protein tyrosine phosphatases are involved in RT abscisic acid-dependent processes in Arabidopsis seeds and suspension RT cells."; RL Plant Physiol. 148:1668-1680(2008). RN [9] RP TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, NOMENCLATURE, AND DISRUPTION RP PHENOTYPE. RX PubMed=22561114; DOI=10.1016/j.gene.2012.04.042; RA Lu W., Tang X., Huo Y., Xu R., Qi S., Huang J., Zheng C., Wu C.A.; RT "Identification and characterization of fructose 1,6-bisphosphate aldolase RT genes in Arabidopsis reveal a gene family with diverse responses to abiotic RT stresses."; RL Gene 503:65-74(2012). RN [10] RP METHYLATION AT LYS-394, MUTAGENESIS OF LYS-394, CATALYTIC ACTIVITY, RP SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22547063; DOI=10.1074/jbc.m112.359976; RA Mininno M., Brugiere S., Pautre V., Gilgen A., Ma S., Ferro M., Tardif M., RA Alban C., Ravanel S.; RT "Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as RT lysine-methylated proteins in plants."; RL J. Biol. Chem. 287:21034-21044(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-215, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22092075; DOI=10.1021/pr200917t; RA Aryal U.K., Krochko J.E., Ross A.R.; RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using RT polyethylene glycol fractionation, immobilized metal-ion affinity RT chromatography, two-dimensional gel electrophoresis and mass RT spectrometry."; RL J. Proteome Res. 11:425-437(2012). CC -!- FUNCTION: Plays a key role in glycolysis and gluconeogenesis. CC {ECO:0000250|UniProtKB:Q9SJQ9}. 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=35 uM for fructose-bisphosphate for the cleavage reaction CC {ECO:0000269|PubMed:22547063}; CC Vmax=13 umol/min/mg enzyme with fructose-bisphosphate as substrate CC {ECO:0000269|PubMed:22547063}; 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:0000269|PubMed:22547063}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule CC {ECO:0000269|PubMed:16414959, ECO:0000269|PubMed:16461379}. Plastid, CC chloroplast stroma {ECO:0000269|PubMed:16414959}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences.; CC Name=1; CC IsoId=Q944G9-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Highly expressed in rosettes leaves. CC {ECO:0000269|PubMed:22561114}. CC -!- INDUCTION: By glucose and sucrose (PubMed:22561114). Induced by drought CC stress (PubMed:22561114). {ECO:0000269|PubMed:22561114}. CC -!- PTM: Can be trimethylated at Lys-394 by LSMT-L. The methylation level CC has no influence on the ologomerization state or on the kinetic CC properties of the enzyme. {ECO:0000269|PubMed:22547063}. CC -!- PTM: Phosphorylated on tyrosine residues in response to abscisic acid CC (ABA) in germinating seeds. {ECO:0000269|PubMed:18768909}. CC -!- DISRUPTION PHENOTYPE: Reduced growth rate. Unability to accumulate CC starch in leaves during daylight. {ECO:0000269|PubMed:22561114}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB38817.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB80560.1; 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; AL035679; CAB38817.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161594; CAB80560.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE87002.1; -; Genomic_DNA. DR EMBL; AF428455; AAL16224.1; -; mRNA. DR EMBL; BT015870; AAU94433.1; -; mRNA. DR EMBL; AK226247; BAE98409.1; -; mRNA. DR PIR; T06057; T06057. DR RefSeq; NP_568049.1; NM_120057.4. [Q944G9-1] DR AlphaFoldDB; Q944G9; -. DR SMR; Q944G9; -. DR BioGRID; 15332; 5. DR STRING; 3702.Q944G9; -. DR iPTMnet; Q944G9; -. DR PaxDb; 3702-AT4G38970-1; -. DR ProteomicsDB; 244954; -. [Q944G9-1] DR EnsemblPlants; AT4G38970.1; AT4G38970.1; AT4G38970. [Q944G9-1] DR GeneID; 830052; -. DR Gramene; AT4G38970.1; AT4G38970.1; AT4G38970. [Q944G9-1] DR KEGG; ath:AT4G38970; -. DR Araport; AT4G38970; -. DR TAIR; AT4G38970; FBA2. DR eggNOG; KOG1557; Eukaryota. DR HOGENOM; CLU_031243_0_0_1; -. DR InParanoid; Q944G9; -. DR OMA; MENTEAN; -. DR OrthoDB; 3595068at2759; -. DR BioCyc; ARA:AT4G38970-MONOMER; -. DR UniPathway; UPA00109; UER00183. DR PRO; PR:Q944G9; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q944G9; baseline and differential. DR GO; GO:0048046; C:apoplast; HDA:TAIR. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0010287; C:plastoglobule; HDA:TAIR. DR GO; GO:0009579; C:thylakoid; HDA:TAIR. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IDA:TAIR. DR GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB. DR GO; GO:0006096; P:glycolytic process; ISS:UniProtKB. DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR. 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:SF64; FRUCTOSE-BISPHOSPHATE ALDOLASE 2, CHLOROPLASTIC; 1. DR Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. DR Genevisible; Q944G9; AT. PE 1: Evidence at protein level; KW Alternative splicing; Chloroplast; Glycolysis; Lyase; Methylation; KW Phosphoprotein; Plastid; Reference proteome; Schiff base; Transit peptide. FT TRANSIT 1..46 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 47..398 FT /note="Fructose-bisphosphate aldolase 2, chloroplastic" FT /id="PRO_0000286527" FT ACT_SITE 225 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00883" FT ACT_SITE 267 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 95 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 185 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 309..311 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00883" FT SITE 398 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT /evidence="ECO:0000250|UniProtKB:P00883" FT MOD_RES 157 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22092075" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22092075" FT MOD_RES 394 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:22547063" FT MUTAGEN 394 FT /note="K->A: Loss of methylation, but no effect on enzyme FT activity." FT /evidence="ECO:0000269|PubMed:22547063" FT CONFLICT 163 FT /note="C -> G (in Ref. 3; AAL16224)" FT /evidence="ECO:0000305" SQ SEQUENCE 398 AA; 42988 MW; E306F39ED18BD71D CRC64; MASTSLLKAS PVLDKSEWVK GQSVLFRQPS SASVVLRNRA TSLTVRAASS YADELVKTAK TIASPGRGIL AMDESNATCG KRLDSIGLEN TEANRQAFRT LLVSAPGLGQ YVSGAILFEE TLYQSTTEGK KMVDVLVEQN IVPGIKVDKG LVPLVGSNNE SWCQGLDGLS SRTAAYYQQG ARFAKWRTVV SIPNGPSALA VKEAAWGLAR YAAISQDSGL VPIVEPEILL DGEHDIDRTY DVAEKVWAEV FFYLAQNNVM FEGILLKPSM VTPGAESKDR ATPEQVAAYT LKLLRNRVPP AVPGIMFLSG GQSEVEATLN LNAMNQAPNP WHVSFSYARA LQNTCLKTWG GRPENVNAAQ TTLLARAKAN SLAQLGKYTG EGESEEAKEG MFVKGYTY //