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 03-AUG-2022, entry version 153.
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}.
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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 AlphaFoldDB; P22197; -.
DR SMR; P22197; -.
DR STRING; 3702.AT4G26520.1; -.
DR PaxDb; P22197; -.
DR PRIDE; P22197; -.
DR ProteomicsDB; 244403; -.
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 HOGENOM; CLU_031243_0_2_1; -.
DR InParanoid; P22197; -.
DR PhylomeDB; P22197; -.
DR BioCyc; ARA:AT4G26520-MON; -.
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 PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 2: Evidence at transcript level;
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 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 /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 266..268
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 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
