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Fructose-bisphosphate aldolase 8, cytosolic (AtFBA8) (EC 4.1.2.13) (Cytosolic aldolase 1) (cAld1)

 ALFC8_ARATH             Reviewed;         358 AA.
Q9LF98;
05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
23-MAY-2018, entry version 146.
RecName: Full=Fructose-bisphosphate aldolase 8, cytosolic {ECO:0000305};
Short=AtFBA8 {ECO:0000303|PubMed:22561114};
EC=4.1.2.13 {ECO:0000250|UniProtKB:Q9SJQ9};
AltName: Full=Cytosolic aldolase 1 {ECO:0000305};
Short=cAld1 {ECO:0000305};
Name=FBA8;
OrderedLocusNames=At3g52930 {ECO:0000312|Araport:AT3G52930};
ORFNames=F8J2_100 {ECO:0000312|EMBL:CAB86897.1};
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=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[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;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[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]
SUBCELLULAR LOCATION.
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]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH TRX3.
PubMed=15352244; DOI=10.1002/pmic.200400805;
Marchand C., Le Marechal P., Meyer Y., Miginiac-Maslow M.,
Issakidis-Bourguet E., Decottignies P.;
"New targets of Arabidopsis thioredoxins revealed by proteomic
analysis.";
Proteomics 4:2696-2706(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND GLUTATHIONYLATION.
PubMed=15734904; DOI=10.1104/pp.104.058719;
Lindermayr C., Saalbach G., Durner J.;
"Proteomic identification of S-nitrosylated proteins in Arabidopsis.";
Plant Physiol. 137:921-930(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[11]
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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Fructose-bisphosphate aldolase that plays a key role in
glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:Q9SJQ9}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
phosphate + D-glyceraldehyde 3-phosphate.
{ECO:0000250|UniProtKB:Q9SJQ9}.
-!- 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 TRX3
(PubMed:15352244). {ECO:0000250|UniProtKB:Q944G9,
ECO:0000269|PubMed:15352244}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:12953116}. Mitochondrion outer membrane
{ECO:0000269|PubMed:12953116}. Note=Found in circular or rod-
shaped bodies that colocalizes with mitochondrion marker.
{ECO:0000269|PubMed:12953116}.
-!- TISSUE SPECIFICITY: Highly expressed in flowers.
{ECO:0000269|PubMed:22561114}.
-!- INDUCTION: By glucose, fructose and sucrose (PubMed:22561114).
Induced by abiotic stresses (PubMed:22561114).
{ECO:0000269|PubMed:22561114}.
-!- PTM: S-glutathionylated at Cys-68 and Cys-173.
{ECO:0000250|UniProtKB:Q9SJQ9}.
-!- PTM: S-nitrosylated at Cys-173. {ECO:0000250|UniProtKB:Q9SJQ9}.
-!- DISRUPTION PHENOTYPE: Sterility. {ECO:0000269|PubMed:22561114}.
-!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL132969; CAB86897.1; -; Genomic_DNA.
EMBL; CP002686; AEE79012.1; -; Genomic_DNA.
EMBL; AY052709; AAK96613.1; -; mRNA.
EMBL; AY057656; AAL15287.1; -; mRNA.
EMBL; AY063718; AAL36068.1; -; mRNA.
EMBL; AK317380; BAH20051.1; -; mRNA.
EMBL; AY087346; AAM64896.1; -; mRNA.
PIR; T47550; T47550.
RefSeq; NP_190861.1; NM_115153.4.
UniGene; At.25299; -.
UniGene; At.75318; -.
ProteinModelPortal; Q9LF98; -.
SMR; Q9LF98; -.
IntAct; Q9LF98; 4.
STRING; 3702.AT3G52930.1; -.
iPTMnet; Q9LF98; -.
PaxDb; Q9LF98; -.
PRIDE; Q9LF98; -.
ProMEX; Q9LF98; -.
EnsemblPlants; AT3G52930.1; AT3G52930.1; AT3G52930.
GeneID; 824459; -.
Gramene; AT3G52930.1; AT3G52930.1; AT3G52930.
KEGG; ath:AT3G52930; -.
Araport; AT3G52930; -.
TAIR; locus:2085141; AT3G52930.
eggNOG; KOG1557; Eukaryota.
eggNOG; COG3588; LUCA.
HOGENOM; HOG000220876; -.
KO; K01623; -.
OMA; MILKPNM; -.
OrthoDB; EOG09360ENE; -.
PhylomeDB; Q9LF98; -.
BioCyc; ARA:AT3G52930-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:Q9LF98; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LF98; differential.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005740; C:mitochondrial envelope; IDA:TAIR.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
GO; GO:0006096; P:glycolytic process; ISS:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0080167; P:response to karrikin; IEP: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; Complete proteome; Cytoplasm; Glutathionylation;
Glycolysis; Lyase; Membrane; Methylation; Mitochondrion;
Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
S-nitrosylation; Schiff base.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 358 Fructose-bisphosphate aldolase 8,
cytosolic.
/FTId=PRO_0000437241.
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:0000244|PubMed:22223895}.
MOD_RES 68 68 S-glutathionyl cysteine; transient.
{ECO:0000250|UniProtKB:Q9SJQ9}.
MOD_RES 173 173 S-glutathionyl cysteine; transient;
alternate.
{ECO:0000250|UniProtKB:Q9SJQ9}.
MOD_RES 173 173 S-nitrosocysteine; transient; alternate.
{ECO:0000250|UniProtKB:Q9SJQ9}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:19245862}.
MOD_RES 354 354 N6,N6,N6-trimethyllysine.
{ECO:0000250|UniProtKB:Q9SJU4}.
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


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