ID ALFP3_ARATH Reviewed; 391 AA.
AC Q9ZU52;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Fructose-bisphosphate aldolase 3, chloroplastic {ECO:0000305};
DE Short=AtFBA3 {ECO:0000303|PubMed:22561114};
DE EC=4.1.2.13 {ECO:0000305};
DE AltName: Full=Protein PIGMENT DEFECTIVE 345;
DE Flags: Precursor;
GN Name=FBA3 {ECO:0000303|PubMed:22561114}; Synonyms=PDE345;
GN OrderedLocusNames=At2g01140; ORFNames=F10A8.2;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DOWN-REGULATION BY OXIDATIVE STRESS.
RX PubMed=12492832; DOI=10.1046/j.1365-313x.2002.01474.x;
RA Sweetlove L.J., Heazlewood J.L., Herald V., Holtzapffel R., Day D.A.,
RA Leaver C.J., Millar A.H.;
RT "The impact of oxidative stress on Arabidopsis mitochondria.";
RL Plant J. 32:891-904(2002).
RN [6]
RP PROTEIN SEQUENCE OF 42-50, AND GLUTATHIONYLATION.
RX PubMed=12881492; DOI=10.1093/pcp/pcg098;
RA Ito H., Iwabuchi M., Ogawa K.;
RT "The sugar-metabolic enzymes aldolase and triose-phosphate isomerase are
RT targets of glutathionylation in Arabidopsis thaliana: detection using
RT biotinylated glutathione.";
RL Plant Cell Physiol. 44:655-660(2003).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [9]
RP TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
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-387.
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).
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 -!- 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: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:16461379}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, and at low levels in rosettes
CC leaves, cauline leaves, stems and flowers.
CC {ECO:0000269|PubMed:22561114}.
CC -!- INDUCTION: Down-regulated by oxidative stress (PubMed:12492832).
CC Induced by fructose and sucrose (PubMed:22561114). Down-regulated by
CC abiotic stresses (PubMed:22561114). {ECO:0000269|PubMed:12492832,
CC ECO:0000269|PubMed:22561114}.
CC -!- PTM: Can be trimethylated at Lys-387 by LSMT-L, but the trimethylation
CC has no effect in vitro. {ECO:0000269|PubMed:22547063}.
CC -!- PTM: S-glutathionylated. {ECO:0000269|PubMed:12881492}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AC006200; AAD14543.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05406.1; -; Genomic_DNA.
DR EMBL; AF325014; AAG40366.1; -; mRNA.
DR EMBL; AY086203; AAM64281.1; -; mRNA.
DR PIR; B84421; B84421.
DR RefSeq; NP_178224.1; NM_126176.5.
DR AlphaFoldDB; Q9ZU52; -.
DR SMR; Q9ZU52; -.
DR BioGRID; 47; 14.
DR IntAct; Q9ZU52; 1.
DR STRING; 3702.Q9ZU52; -.
DR iPTMnet; Q9ZU52; -.
DR PaxDb; 3702-AT2G01140-1; -.
DR ProteomicsDB; 244956; -.
DR EnsemblPlants; AT2G01140.1; AT2G01140.1; AT2G01140.
DR GeneID; 814643; -.
DR Gramene; AT2G01140.1; AT2G01140.1; AT2G01140.
DR KEGG; ath:AT2G01140; -.
DR Araport; AT2G01140; -.
DR TAIR; AT2G01140; PDE345.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; Q9ZU52; -.
DR OMA; NATSWIA; -.
DR OrthoDB; 3595068at2759; -.
DR PhylomeDB; Q9ZU52; -.
DR BioCyc; ARA:AT2G01140-MONOMER; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:Q9ZU52; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU52; baseline and differential.
DR Genevisible; Q9ZU52; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; ISS: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:SF75; FRUCTOSE-BISPHOSPHATE ALDOLASE 3, CHLOROPLASTIC; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Glutathionylation; Glycolysis;
KW Lyase; Methylation; Phosphoprotein; Plastid; Reference proteome;
KW Schiff base; Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..391
FT /note="Fructose-bisphosphate aldolase 3, chloroplastic"
FT /id="PRO_0000286528"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT ACT_SITE 260
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 302..304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT SITE 391
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q944G9"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q944G9"
FT MOD_RES 387
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:22547063"
SQ SEQUENCE 391 AA; 42327 MW; 4512045C1C325D2A CRC64;
MASASFVKPN TLSSPWIGQR SFAHTSASSS PPPRVSFAIR AGAYSDELVK TAKSIASPGR
GILAIDESNA TCGKRLASIG LDNTEDNRQA YRQLLLTTPG LGDYISGSIL FEETLYQSTK
DGKTFVDCLR DANIVPGIKV DKGLSPLAGS NEESWCQGLD GLASRSAEYY KQGARFAKWR
TVVSVPCGPS ALAVKEAAWG LARYAAISQD NGLVPIVEPE ILLDGDHPIE RTLEVAEKVW
SEVFFYLAQN NVMFEGILLK PSMVTPGAEH KNKASPETVA DFTLTMLKRR VPPAVPGIMF
LSGGQSEAEA TLNLNAMNQS PNPWHVSFSY ARALQNSVLR TWQGKPEKIE ASQKALLVRA
KANSLAQLGK YSAEGENEDA KKGMFVKGYT Y
//
