ALFC5_ARATH
ID ALFC5_ARATH Reviewed; 358 AA.
AC O65581;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Fructose-bisphosphate aldolase 5, cytosolic {ECO:0000305};
DE Short=AtFBA5 {ECO:0000303|PubMed:22561114};
DE EC=4.1.2.13 {ECO:0000250|UniProtKB:Q9SJQ9};
GN Name=FBA5 {ECO:0000303|PubMed:22561114};
GN OrderedLocusNames=At4g26530 {ECO:0000312|Araport:AT4G26530};
GN ORFNames=M3E9.40 {ECO:0000312|EMBL:CAA18217.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
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 [5]
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 [6]
RP INDUCTION.
RX PubMed=16797112; DOI=10.1016/j.biochi.2006.04.018;
RA Herbette S., Taconnat L., Hugouvieux V., Piette L., Magniette M.L.,
RA Cuine S., Auroy P., Richaud P., Forestier C., Bourguignon J., Renou J.P.,
RA Vavasseur A., Leonhardt N.;
RT "Genome-wide transcriptome profiling of the early cadmium response of
RT Arabidopsis roots and shoots.";
RL Biochimie 88:1751-1765(2006).
RN [7]
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).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9SJQ9}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves and cauline leaves.
CC {ECO:0000269|PubMed:22561114}.
CC -!- INDUCTION: Down-regulated by cadmium (PubMed:16797112). Induced by
CC sucrose (PubMed:22561114). Induced by abiotic stresses
CC (PubMed:22561114). {ECO:0000269|PubMed:16797112,
CC 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 -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AL022223; CAA18217.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79508.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85214.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85215.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66838.1; -; Genomic_DNA.
DR EMBL; BT002006; AAN72017.1; -; mRNA.
DR EMBL; BT008844; AAP68283.1; -; mRNA.
DR EMBL; AY087376; AAM64926.1; -; mRNA.
DR PIR; T05051; T05051.
DR RefSeq; NP_001031721.1; NM_001036644.2.
DR RefSeq; NP_001328708.1; NM_001341809.1.
DR RefSeq; NP_194383.1; NM_118786.3.
DR AlphaFoldDB; O65581; -.
DR SMR; O65581; -.
DR IntAct; O65581; 3.
DR STRING; 3702.AT4G26530.2; -.
DR iPTMnet; O65581; -.
DR PaxDb; O65581; -.
DR PRIDE; O65581; -.
DR ProMEX; O65581; -.
DR ProteomicsDB; 244985; -.
DR EnsemblPlants; AT4G26530.1; AT4G26530.1; AT4G26530.
DR EnsemblPlants; AT4G26530.2; AT4G26530.2; AT4G26530.
DR EnsemblPlants; AT4G26530.3; AT4G26530.3; AT4G26530.
DR GeneID; 828759; -.
DR Gramene; AT4G26530.1; AT4G26530.1; AT4G26530.
DR Gramene; AT4G26530.2; AT4G26530.2; AT4G26530.
DR Gramene; AT4G26530.3; AT4G26530.3; AT4G26530.
DR KEGG; ath:AT4G26530; -.
DR Araport; AT4G26530; -.
DR TAIR; locus:2131513; AT4G26530.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_2_1; -.
DR InParanoid; O65581; -.
DR OMA; QKDNAGA; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; O65581; -.
DR BioCyc; ARA:AT4G26530-MON; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:O65581; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65581; baseline and differential.
DR GO; GO:0005829; C:cytosol; 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;
KW Phosphoprotein; Reference proteome; S-nitrosylation; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LF98"
FT CHAIN 2..358
FT /note="Fructose-bisphosphate aldolase 5, cytosolic"
FT /id="PRO_0000437239"
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: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:0000250|UniProtKB:Q9LF98"
SQ SEQUENCE 358 AA; 38294 MW; 351B4420956E64C4 CRC64;
MSAFVGKYAD ELIKTAKYIA TPGKGILAAD ESTGTIGKRF ASINVENIES NRQALRELLF
TSPGTFPCLS GVILFEETLY QKTTDGKPFV ELLMENGVIP GIKVDKGVVD LAGTNGETTT
QGLDSLGARC QEYYKAGARF AKWRAVLKIG ATEPSELSIQ ENAKGLARYA IICQENGLVP
IVEPEVLTDG SHDIKKCAAV TETVLAAVYK ALNDHHVLLE GTLLKPNMVT PGSDSPKVAP
EVIAEYTVTA LRRTVPPAVP GIVFLSGGQS EEEATLNLNA MNKLDVLKPW TLTFSFGRAL
QQSTLKAWAG KTENVAKAQA TFLTRCKGNS DATLGKYTGG ASGDSAASES LYEEGYKY
