ALFC4_ARATH
ID ALFC4_ARATH Reviewed; 393 AA.
AC F4KGQ0; Q8LET3; Q8W4G8; Q9LZR9;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Fructose-bisphosphate aldolase 4, cytosolic {ECO:0000305};
DE Short=AtFBA4 {ECO:0000303|PubMed:22561114};
DE EC=4.1.2.13 {ECO:0000250|UniProtKB:Q9SJQ9};
DE AltName: Full=Cytosolic aldolase 3 {ECO:0000305};
DE Short=cAld3 {ECO:0000305};
GN Name=FBA4 {ECO:0000303|PubMed:22561114};
GN OrderedLocusNames=At5g03690 {ECO:0000312|Araport:AT5G03690};
GN ORFNames=F17C15_110 {ECO:0000312|EMBL:CAB82934.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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] (ISOFORM 2).
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] (ISOFORM 1).
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND
RP 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. {ECO:0000250|UniProtKB:Q944G9}.
CC -!- INTERACTION:
CC F4KGQ0; Q9LF98: FBA8; NbExp=8; IntAct=EBI-4442745, EBI-449265;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22561114}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4KGQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4KGQ0-2; Sequence=VSP_058503;
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers.
CC {ECO:0000269|PubMed:22561114}.
CC -!- INDUCTION: By glucose and fructose (PubMed:22561114). Induced by
CC abiotic stresses (PubMed:22561114). {ECO:0000269|PubMed:22561114}.
CC -!- PTM: S-glutathionylated at Cys-207. {ECO:0000250|UniProtKB:Q9SJQ9}.
CC -!- PTM: S-nitrosylated at Cys-207. {ECO:0000250|UniProtKB:Q9SJQ9}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AL162506; CAB82934.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90642.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90643.1; -; Genomic_DNA.
DR EMBL; AY062566; AAL32644.1; -; mRNA.
DR EMBL; AY093359; AAM13358.1; -; mRNA.
DR EMBL; AY085249; AAM62481.1; -; mRNA.
DR PIR; T48396; T48396.
DR RefSeq; NP_568127.1; NM_120450.3. [F4KGQ0-1]
DR RefSeq; NP_850759.1; NM_180428.2. [F4KGQ0-2]
DR AlphaFoldDB; F4KGQ0; -.
DR SMR; F4KGQ0; -.
DR IntAct; F4KGQ0; 1.
DR STRING; 3702.AT5G03690.1; -.
DR iPTMnet; F4KGQ0; -.
DR PaxDb; F4KGQ0; -.
DR PRIDE; F4KGQ0; -.
DR ProteomicsDB; 245027; -. [F4KGQ0-1]
DR EnsemblPlants; AT5G03690.1; AT5G03690.1; AT5G03690. [F4KGQ0-1]
DR EnsemblPlants; AT5G03690.2; AT5G03690.2; AT5G03690. [F4KGQ0-2]
DR GeneID; 831759; -.
DR Gramene; AT5G03690.1; AT5G03690.1; AT5G03690. [F4KGQ0-1]
DR Gramene; AT5G03690.2; AT5G03690.2; AT5G03690. [F4KGQ0-2]
DR KEGG; ath:AT5G03690; -.
DR Araport; AT5G03690; -.
DR TAIR; locus:2144563; AT5G03690.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; F4KGQ0; -.
DR OMA; THQDIAM; -.
DR OrthoDB; 799973at2759; -.
DR UniPathway; UPA00109; UER00183.
DR PRO; PR:F4KGQ0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KGQ0; 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 Alternative splicing; Cytoplasm; Glutathionylation; Glycolysis; Lyase;
KW Reference proteome; S-nitrosylation; Schiff base.
FT CHAIN 1..393
FT /note="Fructose-bisphosphate aldolase 4, cytosolic"
FT /id="PRO_0000437238"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT ACT_SITE 259
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 301..303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT SITE 393
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT MOD_RES 207
FT /note="S-glutathionyl cysteine; transient; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9SJQ9"
FT MOD_RES 207
FT /note="S-nitrosocysteine; transient; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9SJQ9"
FT VAR_SEQ 10..44
FT /note="GKSYFRRTFHSSIIQFHPQLSILIWHRRYSIIRTY -> D (in isoform
FT 2)"
FT /id="VSP_058503"
FT CONFLICT 23
FT /note="I -> V (in Ref. 4; AAM62481)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> I (in Ref. 4; AAM62481)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="G -> R (in Ref. 4; AAM62481)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="Q -> R (in Ref. 3; AAL32644/AAM13358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 42906 MW; 1D6045A5723A1982 CRC64;
MSCFKSKFAG KSYFRRTFHS SIIQFHPQLS ILIWHRRYSI IRTYELIANA AYIGTPGKGI
LAADESTGTI GKRFVSINVE NVESNRRALR ELLFTTPGAL QYISGIILFE ETLYQKTASG
KLFVDVMKEA GVLPGIKVDK GTVELAGTNG ETTTTGLDGL GDRCKKYYEA GARFAKWRAV
LKIGNNEPSE LAIHENAYGL ARYAVICQEN GLVPIVEPEI LVDGSHDIEK CAYVTERVLA
ACYKALSDHH VILEGTLLKP NMVTPGSDSG SKVKPEVIAK HTVRALQRTV PAAVPAVVFL
SGGQSEEEAT VNLNAINQLK GKKPWSLTFS YGRALQQSTL KAWGGKEENV DKAQKAFLAR
AKANSEATLG GYKGDAQLGE GASESLHVKD YKY
