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Fructose-bisphosphate aldolase 6, cytosolic (AtFBA6) (EC 4.1.2.13) (Cytosolic aldolase 2) (cAld2)

 ALFC6_ARATH             Reviewed;         358 AA.
Q9SJQ9;
05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 141.
RecName: Full=Fructose-bisphosphate aldolase 6, cytosolic {ECO:0000305};
Short=AtFBA6 {ECO:0000303|PubMed:22561114};
EC=4.1.2.13 {ECO:0000269|PubMed:21782461};
AltName: Full=Cytosolic aldolase 2 {ECO:0000303|PubMed:21782461};
Short=cAld2 {ECO:0000303|PubMed:21782461};
Name=FBA6 {ECO:0000303|PubMed:22561114};
OrderedLocusNames=At2g36460 {ECO:0000312|Araport:AT2G36460};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=12953116; DOI=10.1105/tpc.012500;
Giege P., Heazlewood J.L., Roessner-Tunali U., Millar A.H.,
Fernie A.R., Leaver C.J., Sweetlove L.J.;
"Enzymes of glycolysis are functionally associated with the
mitochondrion in Arabidopsis cells.";
Plant Cell 15:2140-2151(2003).
[7]
INDUCTION BY CADMIUM.
STRAIN=cv. Columbia;
PubMed=16502469; DOI=10.1002/pmic.200500543;
Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B.,
Moulin C., Ezan E., Garin J., Bourguignon J.;
"The early responses of Arabidopsis thaliana cells to cadmium exposure
explored by protein and metabolite profiling analyses.";
Proteomics 6:2180-2198(2006).
[8]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, INTERACTION WITH TRX1 AND TRX3, SUBCELLULAR LOCATION,
IDENTIFICATION BY MASS SPECTROMETRY, GLUTATHIONYLATION AT CYS-68 AND
CYS-173, AND S-NITROSYLATION AT CYS-173.
PubMed=21782461; DOI=10.1016/j.plaphy.2011.06.009;
van der Linde K., Gutsche N., Leffers H.M., Lindermayr C., Mueller B.,
Holtgrefe S., Scheibe R.;
"Regulation of plant cytosolic aldolase functions by redox-
modifications.";
Plant Physiol. Biochem. 49:946-957(2011).
[9]
FUNCTION, AND INTERACTION WITH GAPC1 AND VDAC3.
PubMed=23316205; DOI=10.3389/fpls.2012.00284;
Wojtera-Kwiczor J., Gross F., Leffers H.M., Kang M., Schneider M.,
Scheibe R.;
"Transfer of a redox-signal through the cytosol by redox-dependent
microcompartmentation of glycolytic enzymes at mitochondria and actin
cytoskeleton.";
Front. Plant Sci. 3:284-284(2012).
[10]
TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, NOMENCLATURE, AND
DISRUPTION PHENOTYPE.
PubMed=22561114; DOI=10.1016/j.gene.2012.04.042;
Lu W., Tang X., Huo Y., Xu R., Qi S., Huang J., Zheng C., Wu C.A.;
"Identification and characterization of fructose 1,6-bisphosphate
aldolase genes in Arabidopsis reveal a gene family with diverse
responses to abiotic stresses.";
Gene 503:65-74(2012).
-!- FUNCTION: Fructose-bisphosphate aldolase that plays a key role in
glycolysis and gluconeogenesis (PubMed:21782461). Associates with
GAPC1 to the outer mitochondrial membrane, in a redox-dependent
manner, leading to binding and bundling of actin. Actin binding
and bundling occurs under oxidizing conditions and is reversible
under reducing conditions. May be part of a redox-dependent
retrograde signal transduction network for adaptation upon
oxidative stress (PubMed:23316205). {ECO:0000269|PubMed:21782461,
ECO:0000269|PubMed:23316205}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
phosphate + D-glyceraldehyde 3-phosphate.
{ECO:0000269|PubMed:21782461}.
-!- ENZYME REGULATION: Total and irreversible inhibition by S-
nitrosoglutathione (GSNO) (PubMed:21782461). Partial and
reversible inhibition by oxidized glutathione (GSSG)
(PubMed:21782461). {ECO:0000269|PubMed:21782461}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=25 uM for fructose 1,6-bisphosphate
{ECO:0000269|PubMed:21782461};
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 4/4.
{ECO:0000305}.
-!- SUBUNIT: Homotetramer (By similarity). Interacts with TRX1 and
TRX3 (PubMed:21782461). Interacts with GAPC1 AND VDAC3
(PubMed:23316205). {ECO:0000250|UniProtKB:Q944G9,
ECO:0000269|PubMed:21782461, ECO:0000269|PubMed:23316205}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:21782461}. Nucleus
{ECO:0000269|PubMed:21782461}. Mitochondrion
{ECO:0000269|PubMed:12953116}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences. {ECO:0000305};
Name=1;
IsoId=Q9SJQ9-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Expressed in roots, rosettes leaves, cauline
leaves, stems and flowers. {ECO:0000269|PubMed:22561114}.
-!- INDUCTION: By glucose, fructose and sucrose (PubMed:22561114).
Induced by abiotic stresses (PubMed:22561114). Induced by cadmium
(PubMed:16502469). {ECO:0000269|PubMed:16502469,
ECO:0000269|PubMed:22561114}.
-!- PTM: S-glutathionylated at Cys-68 and Cys-173.
{ECO:0000269|PubMed:21782461}.
-!- PTM: S-nitrosylated at Cys-173. {ECO:0000269|PubMed:21782461}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but mutant seeds have increased germination rate in
presence of high salt or high mannitol, and decreased germination
rate in presence of abscisic acid (ABA), glucose, fructose and
sucrose. {ECO:0000269|PubMed:22561114}.
-!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC006919; AAD24630.1; -; Genomic_DNA.
EMBL; CP002685; AEC09256.1; -; Genomic_DNA.
EMBL; AY034897; AAK59404.1; -; mRNA.
EMBL; AY063044; AAL34218.1; -; mRNA.
EMBL; AK226842; BAE98935.1; -; mRNA.
EMBL; AY085114; AAM61668.1; -; mRNA.
PIR; A84781; A84781.
RefSeq; NP_181187.1; NM_129203.3. [Q9SJQ9-1]
UniGene; At.23119; -.
ProteinModelPortal; Q9SJQ9; -.
SMR; Q9SJQ9; -.
IntAct; Q9SJQ9; 1.
STRING; 3702.AT2G36460.1; -.
iPTMnet; Q9SJQ9; -.
SwissPalm; Q9SJQ9; -.
PaxDb; Q9SJQ9; -.
PRIDE; Q9SJQ9; -.
EnsemblPlants; AT2G36460.1; AT2G36460.1; AT2G36460. [Q9SJQ9-1]
GeneID; 818220; -.
Gramene; AT2G36460.1; AT2G36460.1; AT2G36460. [Q9SJQ9-1]
KEGG; ath:AT2G36460; -.
Araport; AT2G36460; -.
TAIR; locus:2044856; AT2G36460.
eggNOG; KOG1557; Eukaryota.
eggNOG; COG3588; LUCA.
HOGENOM; HOG000220876; -.
KO; K01623; -.
OMA; NKPWKLS; -.
OrthoDB; EOG09360ENE; -.
PhylomeDB; Q9SJQ9; -.
BioCyc; ARA:AT2G36460-MONOMER; -.
Reactome; R-ATH-114608; Platelet degranulation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-70171; Glycolysis.
Reactome; R-ATH-70263; Gluconeogenesis.
Reactome; R-ATH-70350; Fructose catabolism.
UniPathway; UPA00109; UER00183.
PRO; PR:Q9SJQ9; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9SJQ9; baseline and differential.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
GO; GO:0006094; P:gluconeogenesis; IDA:UniProtKB.
GO; GO:0006096; P:glycolytic process; IDA:UniProtKB.
GO; GO:0031930; P:mitochondria-nucleus signaling pathway; IDA:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR029768; Aldolase_I_AS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000741; FBA_I.
Pfam; PF00274; Glycolytic; 1.
PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Glutathionylation; Glycolysis; Lyase; Methylation; Mitochondrion;
Nucleus; Phosphoprotein; Reference proteome; S-nitrosylation;
Schiff base; Stress response.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9LF98}.
CHAIN 2 358 Fructose-bisphosphate aldolase 6,
cytosolic.
/FTId=PRO_0000437240.
REGION 266 268 Substrate binding.
{ECO:0000250|UniProtKB:P00883}.
ACT_SITE 183 183 Proton acceptor.
{ECO:0000250|UniProtKB:P00883}.
ACT_SITE 225 225 Schiff-base intermediate with
dihydroxyacetone-P.
{ECO:0000250|UniProtKB:P00883}.
BINDING 39 39 Substrate.
{ECO:0000250|UniProtKB:P00883}.
BINDING 298 298 Substrate.
{ECO:0000250|UniProtKB:P00883}.
SITE 358 358 Necessary for preference for fructose
1,6-bisphosphate over fructose 1-
phosphate.
{ECO:0000250|UniProtKB:P00883}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q9LF98}.
MOD_RES 68 68 S-glutathionyl cysteine; transient.
{ECO:0000269|PubMed:21782461}.
MOD_RES 173 173 S-glutathionyl cysteine; transient;
alternate. {ECO:0000269|PubMed:21782461}.
MOD_RES 173 173 S-nitrosocysteine; transient; alternate.
{ECO:0000269|PubMed:21782461}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000250|UniProtKB:Q9LF98}.
MOD_RES 354 354 N6,N6,N6-trimethyllysine.
{ECO:0000250|UniProtKB:Q9SJU4}.
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


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