(data stored in SCRATCH zone)

SWISSPROT: ALFC7_ARATH

ID   ALFC7_ARATH             Reviewed;         358 AA.
AC   P22197; O65582; Q53YH0;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   11-DEC-2019, entry version 145.
DE   RecName: Full=Fructose-bisphosphate aldolase 7, cytosolic {ECO:0000305};
DE            Short=AtFBA7 {ECO:0000303|PubMed:22561114};
DE            EC=4.1.2.13 {ECO:0000305};
GN   Name=FBA7 {ECO:0000303|PubMed:22561114}; OrderedLocusNames=At4g26520;
GN   ORFNames=M3E9.50;
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 [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=2103470; DOI=10.1007/bf00019171;
RA   Chopra S., Dolferus R., Jacobs M.;
RT   "Cloning and sequencing of the Arabidopsis aldolase gene.";
RL   Plant Mol. Biol. 15:517-520(1990).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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: Plays a key role in glycolysis and gluconeogenesis.
CC       {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. {ECO:0000250|UniProtKB:Q944G9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9SJQ9}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in flowers, and at lower levels in
CC       rosettes leaves and cauline leaves. {ECO:0000269|PubMed:22561114}.
CC   -!- INDUCTION: Down-regulated by cadmium (PubMed:16797112). Induced by
CC       glucose and sucrose (PubMed:22561114). Induced by drought stress
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; X53058; CAA37226.1; -; Genomic_DNA.
DR   EMBL; AL022223; CAA18218.1; -; Genomic_DNA.
DR   EMBL; AL161565; CAB79507.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85213.1; -; Genomic_DNA.
DR   EMBL; BT001927; AAN71926.1; -; mRNA.
DR   PIR; D85307; D85307.
DR   PIR; S11958; ADMU.
DR   RefSeq; NP_194382.1; NM_118785.4.
DR   SMR; P22197; -.
DR   STRING; 3702.AT4G26520.1; -.
DR   PaxDb; P22197; -.
DR   PRIDE; P22197; -.
DR   EnsemblPlants; AT4G26520.1; AT4G26520.1; AT4G26520.
DR   GeneID; 828758; -.
DR   Gramene; AT4G26520.1; AT4G26520.1; AT4G26520.
DR   KEGG; ath:AT4G26520; -.
DR   Araport; AT4G26520; -.
DR   TAIR; locus:2131508; AT4G26520.
DR   eggNOG; KOG1557; Eukaryota.
DR   eggNOG; COG3588; LUCA.
DR   HOGENOM; HOG000220876; -.
DR   InParanoid; P22197; -.
DR   KO; K01623; -.
DR   OrthoDB; 799973at2759; -.
DR   PhylomeDB; P22197; -.
DR   BioCyc; ARA:AT4G26520-MONOMER; -.
DR   UniPathway; UPA00109; UER00183.
DR   PRO; PR:P22197; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P22197; baseline and differential.
DR   Genevisible; P22197; AT.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   GO; GO:0001666; P:response to hypoxia; IEP:TAIR.
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   2: Evidence at transcript level;
DR   PRODOM; P22197.
DR   SWISS-2DPAGE; P22197.
KW   Acetylation; Cytoplasm; Glutathionylation; Glycolysis; Lyase;
KW   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 7, cytosolic"
FT                   /id="PRO_0000216919"
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         52
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         142
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   CONFLICT        138
FT                   /note="A -> G (in Ref. 1; CAA37226)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   358 AA;  38810 MW;  3588E066D488C9CB CRC64;
     MSAFVSKYED ELIKTAKYIA TPGRGILAAD ESTETIGKRF AGINVENTES NRQAYRELLF
     TSPGSYPCLS GVILFEETLY QKTSDGKPFV DLLMENGVIP GIKVDKGLVD LAGTNGETTT
     QGLDSLGARC QQYYEAGARF AKWRAFFKIG ATEPSVLSIQ EDARVLARYA IICQENGLVP
     IVEPEVLTGG SHDIKKCAAV TETVLAAVFK ALNYHHVLLE GTLLKPNMVT PGSDSPKVAP
     ELIAEYTVTA LRRTVPPAIP GIVFLSGIQR EEQATLNLNA MNKLDVLKPW TLTFSFGGAL
     QQSAIKAWAG KPENVAKAQA KFLTRCKANK DATLGKYTGW ASGDSAAFEN LVVIGYRY
//

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