ALFC6_ARATH
ID ALFC6_ARATH Reviewed; 358 AA.
AC Q9SJQ9;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Fructose-bisphosphate aldolase 6, cytosolic {ECO:0000305};
DE Short=AtFBA6 {ECO:0000303|PubMed:22561114};
DE EC=4.1.2.13 {ECO:0000269|PubMed:21782461};
DE AltName: Full=Cytosolic aldolase 2 {ECO:0000303|PubMed:21782461};
DE Short=cAld2 {ECO:0000303|PubMed:21782461};
GN Name=FBA6 {ECO:0000303|PubMed:22561114};
GN OrderedLocusNames=At2g36460 {ECO:0000312|Araport:AT2G36460};
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].
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 [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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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 INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, INTERACTION WITH TRX1 AND TRX3, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, GLUTATHIONYLATION AT CYS-68 AND
RP CYS-173, AND S-NITROSYLATION AT CYS-173.
RX PubMed=21782461; DOI=10.1016/j.plaphy.2011.06.009;
RA van der Linde K., Gutsche N., Leffers H.M., Lindermayr C., Mueller B.,
RA Holtgrefe S., Scheibe R.;
RT "Regulation of plant cytosolic aldolase functions by redox-modifications.";
RL Plant Physiol. Biochem. 49:946-957(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH GAPC1 AND VDAC3.
RX PubMed=23316205; DOI=10.3389/fpls.2012.00284;
RA Wojtera-Kwiczor J., Gross F., Leffers H.M., Kang M., Schneider M.,
RA Scheibe R.;
RT "Transfer of a redox-signal through the cytosol by redox-dependent
RT microcompartmentation of glycolytic enzymes at mitochondria and actin
RT cytoskeleton.";
RL Front. Plant Sci. 3:284-284(2012).
RN [10]
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).
CC -!- FUNCTION: Fructose-bisphosphate aldolase that plays a key role in
CC glycolysis and gluconeogenesis (PubMed:21782461). Associates with GAPC1
CC to the outer mitochondrial membrane, in a redox-dependent manner,
CC leading to binding and bundling of actin. Actin binding and bundling
CC occurs under oxidizing conditions and is reversible under reducing
CC conditions. May be part of a redox-dependent retrograde signal
CC transduction network for adaptation upon oxidative stress
CC (PubMed:23316205). {ECO:0000269|PubMed:21782461,
CC ECO:0000269|PubMed:23316205}.
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:0000269|PubMed:21782461};
CC -!- ACTIVITY REGULATION: Total and irreversible inhibition by S-
CC nitrosoglutathione (GSNO) (PubMed:21782461). Partial and reversible
CC inhibition by oxidized glutathione (GSSG) (PubMed:21782461).
CC {ECO:0000269|PubMed:21782461}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:21782461};
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 TRX1 and TRX3
CC (PubMed:21782461). Interacts with GAPC1 AND VDAC3 (PubMed:23316205).
CC {ECO:0000250|UniProtKB:Q944G9, ECO:0000269|PubMed:21782461,
CC ECO:0000269|PubMed:23316205}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21782461}.
CC Nucleus {ECO:0000269|PubMed:21782461}. Mitochondrion
CC {ECO:0000269|PubMed:12953116}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9SJQ9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosettes leaves, cauline
CC leaves, stems and flowers. {ECO:0000269|PubMed:22561114}.
CC -!- INDUCTION: By glucose, fructose and sucrose (PubMed:22561114). Induced
CC by abiotic stresses (PubMed:22561114). Induced by cadmium
CC (PubMed:16502469). {ECO:0000269|PubMed:16502469,
CC ECO:0000269|PubMed:22561114}.
CC -!- PTM: S-glutathionylated at Cys-68 and Cys-173.
CC {ECO:0000269|PubMed:21782461}.
CC -!- PTM: S-nitrosylated at Cys-173. {ECO:0000269|PubMed:21782461}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seeds have increased germination rate in
CC presence of high salt or high mannitol, and decreased germination rate
CC in presence of abscisic acid (ABA), glucose, fructose and sucrose.
CC {ECO:0000269|PubMed:22561114}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AC006919; AAD24630.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09256.1; -; Genomic_DNA.
DR EMBL; AY034897; AAK59404.1; -; mRNA.
DR EMBL; AY063044; AAL34218.1; -; mRNA.
DR EMBL; AK226842; BAE98935.1; -; mRNA.
DR EMBL; AY085114; AAM61668.1; -; mRNA.
DR PIR; A84781; A84781.
DR RefSeq; NP_181187.1; NM_129203.3. [Q9SJQ9-1]
DR PDB; 6RNG; X-ray; 2.15 A; A/B/F/G=1-358.
DR PDB; 6RS1; X-ray; 1.90 A; A/B/C/D=1-358.
DR PDBsum; 6RNG; -.
DR PDBsum; 6RS1; -.
DR AlphaFoldDB; Q9SJQ9; -.
DR SMR; Q9SJQ9; -.
DR IntAct; Q9SJQ9; 1.
DR STRING; 3702.AT2G36460.1; -.
DR iPTMnet; Q9SJQ9; -.
DR MetOSite; Q9SJQ9; -.
DR SwissPalm; Q9SJQ9; -.
DR PaxDb; Q9SJQ9; -.
DR PRIDE; Q9SJQ9; -.
DR ProteomicsDB; 244903; -. [Q9SJQ9-1]
DR EnsemblPlants; AT2G36460.1; AT2G36460.1; AT2G36460. [Q9SJQ9-1]
DR GeneID; 818220; -.
DR Gramene; AT2G36460.1; AT2G36460.1; AT2G36460. [Q9SJQ9-1]
DR KEGG; ath:AT2G36460; -.
DR Araport; AT2G36460; -.
DR TAIR; locus:2044856; AT2G36460.
DR eggNOG; KOG1557; Eukaryota.
DR InParanoid; Q9SJQ9; -.
DR OMA; GALPCIS; -.
DR PhylomeDB; Q9SJQ9; -.
DR BioCyc; ARA:AT2G36460-MON; -.
DR SABIO-RK; Q9SJQ9; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:Q9SJQ9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJQ9; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IDA:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IDA:UniProtKB.
DR GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IDA: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 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Glutathionylation; Glycolysis; Lyase; Methylation; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; S-nitrosylation; Schiff base;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LF98"
FT CHAIN 2..358
FT /note="Fructose-bisphosphate aldolase 6, cytosolic"
FT /id="PRO_0000437240"
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:0000250|UniProtKB:Q9LF98"
FT MOD_RES 68
FT /note="S-glutathionyl cysteine; transient"
FT /evidence="ECO:0000269|PubMed:21782461"
FT MOD_RES 173
FT /note="S-glutathionyl cysteine; transient; alternate"
FT /evidence="ECO:0000269|PubMed:21782461"
FT MOD_RES 173
FT /note="S-nitrosocysteine; transient; alternate"
FT /evidence="ECO:0000269|PubMed:21782461"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LF98"
FT MOD_RES 354
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9SJU4"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:6RS1"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:6RS1"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 156..175
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 194..214
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 271..282
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:6RS1"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:6RNG"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:6RS1"
FT HELIX 315..333
FT /evidence="ECO:0007829|PDB:6RS1"
SQ SEQUENCE 358 AA; 38387 MW; 0426179B1F27B5A6 CRC64;
MSSFTSKFAD ELIANAAYIG TPGKGILAAD ESTGTIGKRL ASINVENVES NRRALRELLF
TTPGALPCLS GVILFEETLY QKSSDGTPFV DMLKSAGVLP GIKVDKGTVE LAGTNGETTT
QGLDGLGDRC KKYYEAGARF AKWRAVLKIG VNEPSQLAIH ENAYGLARYA VICQENGLVP
IVEPEILVDG SHDIQKCAAV TERVLAACYK ALSDHHVLLE GTLLKPNMVT PGSESAKVAP
EVIAEHTVRA LQRTVPAAVP AIVFLSGGQS EEEATRNLNA MNQLKTKKPW SLSFSFGRAL
QQSTLKTWGG KEENVKKAQE AFLVRCKANS EATLGAYKGD AKLGEGAAES LHVKDYKY
