(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 157.
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}.
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   SMR; O65581; -.
DR   IntAct; O65581; 3.
DR   STRING; 3702.AT4G26530.2; -.
DR   iPTMnet; O65581; -.
DR   PaxDb; O65581; -.
DR   PRIDE; O65581; -.
DR   ProMEX; O65581; -.
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   eggNOG; COG3588; LUCA.
DR   HOGENOM; HOG000220876; -.
DR   InParanoid; O65581; -.
DR   KO; K01623; -.
DR   OMA; PLCKPWA; -.
DR   OrthoDB; 799973at2759; -.
DR   PhylomeDB; O65581; -.
DR   BioCyc; ARA:AT4G26530-MONOMER; -.
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: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   Pfam; PF00274; Glycolytic; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O65581.
DR   SWISS-2DPAGE; O65581.
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   REGION          266..268
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
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                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         298
FT                   /note="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
//

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