ALFP1_ARATH
ID ALFP1_ARATH Reviewed; 399 AA.
AC Q9SJU4; Q2V473; Q93WF5; Q94C97;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Fructose-bisphosphate aldolase 1, chloroplastic {ECO:0000305};
DE Short=AtFBA1 {ECO:0000303|PubMed:22561114};
DE EC=4.1.2.13 {ECO:0000305};
DE Flags: Precursor;
GN Name=FBA1 {ECO:0000303|PubMed:22561114}; OrderedLocusNames=At2g21330;
GN ORFNames=F3K23.9;
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 PROTEIN SEQUENCE OF 49-60, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND GLUTATHIONYLATION.
RX PubMed=15734904; DOI=10.1104/pp.104.058719;
RA Lindermayr C., Saalbach G., Durner J.;
RT "Proteomic identification of S-nitrosylated proteins in Arabidopsis.";
RL Plant Physiol. 137:921-930(2005).
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 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 [9]
RP METHYLATION AT LYS-395.
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:11719511, ECO:0000269|PubMed:16414959,
CC ECO:0000269|PubMed:16461379}. Plastid, chloroplast stroma
CC {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=Q9SJU4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in rosettes leaves and cauline
CC leaves. {ECO:0000269|PubMed:22561114}.
CC -!- INDUCTION: By sucrose (PubMed:22561114). Induced by drought stress
CC (PubMed:22561114). {ECO:0000269|PubMed:22561114}.
CC -!- PTM: Can be trimethylated at Lys-395 by LSMT-L, but the trimethylation
CC has no effect in vitro on the kinetic properties of the enzyme.
CC {ECO:0000269|PubMed:22547063}.
CC -!- PTM: S-glutathionylated. {ECO:0000269|PubMed:15734904}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AC006841; AAD23681.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07160.1; -; Genomic_DNA.
DR EMBL; AF419589; AAL31921.1; -; mRNA.
DR EMBL; AF428408; AAL16176.1; -; mRNA.
DR EMBL; AY035043; AAK59548.1; -; mRNA.
DR EMBL; AY049282; AAK83624.1; -; mRNA.
DR EMBL; AY049286; AAK83628.1; -; mRNA.
DR EMBL; AY062582; AAL32660.1; -; mRNA.
DR EMBL; AY090291; AAL90952.1; -; mRNA.
DR EMBL; AY128380; AAM91583.1; -; mRNA.
DR EMBL; AY128784; AAM91184.1; -; mRNA.
DR EMBL; AY142633; AAN13091.1; -; mRNA.
DR EMBL; BT000106; AAN15425.1; -; mRNA.
DR EMBL; BT002415; AAO00775.1; -; mRNA.
DR PIR; A84600; A84600.
DR RefSeq; NP_565508.1; NM_127705.4. [Q9SJU4-1]
DR AlphaFoldDB; Q9SJU4; -.
DR SMR; Q9SJU4; -.
DR BioGRID; 2025; 3.
DR STRING; 3702.AT2G21330.1; -.
DR iPTMnet; Q9SJU4; -.
DR World-2DPAGE; 0003:Q9SJU4; -.
DR PaxDb; Q9SJU4; -.
DR PRIDE; Q9SJU4; -.
DR ProteomicsDB; 245045; -. [Q9SJU4-1]
DR EnsemblPlants; AT2G21330.1; AT2G21330.1; AT2G21330. [Q9SJU4-1]
DR GeneID; 816672; -.
DR Gramene; AT2G21330.1; AT2G21330.1; AT2G21330. [Q9SJU4-1]
DR KEGG; ath:AT2G21330; -.
DR Araport; AT2G21330; -.
DR TAIR; locus:2050049; AT2G21330.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; Q9SJU4; -.
DR OMA; EVASMVW; -.
DR PhylomeDB; Q9SJU4; -.
DR BioCyc; ARA:AT2G21330-MON; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:Q9SJU4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJU4; baseline and differential.
DR Genevisible; Q9SJU4; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
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 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; Direct protein sequencing;
KW Glutathionylation; Glycolysis; Lyase; Methylation; Phosphoprotein; Plastid;
KW Reference proteome; Schiff base; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 49..399
FT /note="Fructose-bisphosphate aldolase 1, chloroplastic"
FT /id="PRO_0000286526"
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT ACT_SITE 268
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 310..312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT SITE 399
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q944G9"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q944G9"
FT MOD_RES 395
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:22547063"
FT CONFLICT 236
FT /note="G -> S (in Ref. 3; AAK59548)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="E -> G (in Ref. 3; AAK59548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 42931 MW; 26CC71FA3C571B53 CRC64;
MASSTATMLK ASPVKSDWVK GQSLLLRQPS SVSAIRSHVA PSALTVRAAS AYADELVKTA
KTIASPGHGI MAMDESNATC GKRLASIGLE NTEANRQAYR TLLVSAPGLG QYISGAILFE
ETLYQSTTDG KKMVDVLVEQ NIVPGIKVDK GLVPLVGSYD ESWCQGLDGL ASRTAAYYQQ
GARFAKWRTV VSIPNGPSAL AVKEAAWGLA RYAAISQDSG LVPIVEPEIM LDGEHGIDRT
YDVAEKVWAE VFFYLAQNNV MFEGILLKPS MVTPGAEATD RATPEQVASY TLKLLRNRIP
PAVPGIMFLS GGQSELEATL NLNAMNQAPN PWHVSFSYAR ALQNTCLKTW GGKEENVKAA
QDILLARAKA NSLAQLGKYT GEGESEEAKE GMFVKGYTY
