ALFC8_ARATH
ID ALFC8_ARATH Reviewed; 358 AA.
AC Q9LF98;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Fructose-bisphosphate aldolase 8, cytosolic {ECO:0000305};
DE Short=AtFBA8 {ECO:0000303|PubMed:22561114};
DE EC=4.1.2.13 {ECO:0000250|UniProtKB:Q9SJQ9};
DE AltName: Full=Cytosolic aldolase 1 {ECO:0000305};
DE Short=cAld1 {ECO:0000305};
GN Name=FBA8; OrderedLocusNames=At3g52930 {ECO:0000312|Araport:AT3G52930};
GN ORFNames=F8J2_100 {ECO:0000312|EMBL:CAB86897.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12953116; DOI=10.1105/tpc.012500;
RA Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H., Fernie A.R.,
RA Leaver C.J., Sweetlove L.J.;
RT "Enzymes of glycolysis are functionally associated with the mitochondrion
RT in Arabidopsis cells.";
RL Plant Cell 15:2140-2151(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH TRX3.
RX PubMed=15352244; DOI=10.1002/pmic.200400805;
RA Marchand C., Le Marechal P., Meyer Y., Miginiac-Maslow M.,
RA Issakidis-Bourguet E., Decottignies P.;
RT "New targets of Arabidopsis thioredoxins revealed by proteomic analysis.";
RL Proteomics 4:2696-2706(2004).
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Fructose-bisphosphate aldolase that plays a key role in
CC glycolysis and gluconeogenesis. {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 (By similarity). Interacts with TRX3
CC (PubMed:15352244). {ECO:0000250|UniProtKB:Q944G9,
CC ECO:0000269|PubMed:15352244}.
CC -!- INTERACTION:
CC Q9LF98; F4KGQ0: FBA4; NbExp=8; IntAct=EBI-449265, EBI-4442745;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12953116}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:12953116}. Note=Found
CC in circular or rod-shaped bodies that colocalizes with mitochondrion
CC marker. {ECO:0000269|PubMed:12953116}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers.
CC {ECO:0000269|PubMed:22561114}.
CC -!- INDUCTION: By glucose, fructose and sucrose (PubMed:22561114). Induced
CC by abiotic stresses (PubMed:22561114). {ECO:0000269|PubMed:22561114}.
CC -!- PTM: S-glutathionylated at Cys-68 and Cys-173.
CC {ECO:0000250|UniProtKB:Q9SJQ9}.
CC -!- PTM: S-nitrosylated at Cys-173. {ECO:0000250|UniProtKB:Q9SJQ9}.
CC -!- DISRUPTION PHENOTYPE: Sterility. {ECO:0000269|PubMed:22561114}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AL132969; CAB86897.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79012.1; -; Genomic_DNA.
DR EMBL; AY052709; AAK96613.1; -; mRNA.
DR EMBL; AY057656; AAL15287.1; -; mRNA.
DR EMBL; AY063718; AAL36068.1; -; mRNA.
DR EMBL; AK317380; BAH20051.1; -; mRNA.
DR EMBL; AY087346; AAM64896.1; -; mRNA.
DR PIR; T47550; T47550.
DR RefSeq; NP_190861.1; NM_115153.4.
DR AlphaFoldDB; Q9LF98; -.
DR SMR; Q9LF98; -.
DR IntAct; Q9LF98; 4.
DR STRING; 3702.AT3G52930.1; -.
DR iPTMnet; Q9LF98; -.
DR MetOSite; Q9LF98; -.
DR PaxDb; Q9LF98; -.
DR PRIDE; Q9LF98; -.
DR ProMEX; Q9LF98; -.
DR ProteomicsDB; 245075; -.
DR EnsemblPlants; AT3G52930.1; AT3G52930.1; AT3G52930.
DR GeneID; 824459; -.
DR Gramene; AT3G52930.1; AT3G52930.1; AT3G52930.
DR KEGG; ath:AT3G52930; -.
DR Araport; AT3G52930; -.
DR TAIR; locus:2085141; AT3G52930.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_2_1; -.
DR InParanoid; Q9LF98; -.
DR OMA; CPKKYSP; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; Q9LF98; -.
DR BioCyc; ARA:AT3G52930-MON; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:Q9LF98; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LF98; baseline and differential.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; 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 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 Acetylation; Cytoplasm; Glutathionylation; Glycolysis; Lyase; Membrane;
KW Methylation; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; S-nitrosylation; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..358
FT /note="Fructose-bisphosphate aldolase 8, cytosolic"
FT /id="PRO_0000437241"
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 68
FT /note="S-glutathionyl cysteine; transient"
FT /evidence="ECO:0000250|UniProtKB:Q9SJQ9"
FT MOD_RES 173
FT /note="S-glutathionyl cysteine; transient; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9SJQ9"
FT MOD_RES 173
FT /note="S-nitrosocysteine; transient; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9SJQ9"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 354
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9SJU4"
SQ SEQUENCE 358 AA; 38540 MW; 0E25995B2EE0A319 CRC64;
MSAFTSKFAD ELIANAAYIG TPGKGILAAD ESTGTIGKRL ASINVENVET NRRNLRELLF
TAPGALPCLS GVILFEETLY QKSSDGKLFV DILKEGGVLP GIKVDKGTVE LAGTDGETTT
QGLDGLGDRC KKYYEAGARF AKWRAVLKIG ENEPSEHSIH ENAYGLARYA VICQENGLVP
IVEPEILVDG SHDIQKCAAV TERVLAACYK ALSDHHVLLE GTLLKPNMVT PGSDSPKVSP
EVIAEHTVRA LQRTVPAAVP AIVFLSGGQS EEEATRNLNA MNQLKTKKPW SLSFSFGRAL
QQSTLKTWAG KEENVKAAQE ALYVRCKANS EATLGTYKGD AKLGDGAAES LHVKDYKY
