ALFP2_ARATH
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 03-AUG-2022, entry version 130.
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};
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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.AT4G38970.1; -.
DR iPTMnet; Q944G9; -.
DR PaxDb; Q944G9; -.
DR PRIDE; Q944G9; -.
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; locus:2120192; AT4G38970.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; Q944G9; -.
DR OMA; MENTEAN; -.
DR BioCyc; ARA:AT4G38970-MON; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:Q944G9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q944G9; baseline and differential.
DR Genevisible; Q944G9; AT.
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:0005829; C:cytosol; IBA:GO_Central.
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: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:0009737; P:response to abscisic acid; IEP:TAIR.
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 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
