位置:首页 > 蛋白库 > ALFP3_ARATH
ALFP3_ARATH
ID   ALFP3_ARATH             Reviewed;         391 AA.
AC   Q9ZU52;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Fructose-bisphosphate aldolase 3, chloroplastic {ECO:0000305};
DE            Short=AtFBA3 {ECO:0000303|PubMed:22561114};
DE            EC=4.1.2.13 {ECO:0000305};
DE   AltName: Full=Protein PIGMENT DEFECTIVE 345;
DE   Flags: Precursor;
GN   Name=FBA3 {ECO:0000303|PubMed:22561114}; Synonyms=PDE345;
GN   OrderedLocusNames=At2g01140; ORFNames=F10A8.2;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   DOWN-REGULATION BY OXIDATIVE STRESS.
RX   PubMed=12492832; DOI=10.1046/j.1365-313x.2002.01474.x;
RA   Sweetlove L.J., Heazlewood J.L., Herald V., Holtzapffel R., Day D.A.,
RA   Leaver C.J., Millar A.H.;
RT   "The impact of oxidative stress on Arabidopsis mitochondria.";
RL   Plant J. 32:891-904(2002).
RN   [6]
RP   PROTEIN SEQUENCE OF 42-50, AND GLUTATHIONYLATION.
RX   PubMed=12881492; DOI=10.1093/pcp/pcg098;
RA   Ito H., Iwabuchi M., Ogawa K.;
RT   "The sugar-metabolic enzymes aldolase and triose-phosphate isomerase are
RT   targets of glutathionylation in Arabidopsis thaliana: detection using
RT   biotinylated glutathione.";
RL   Plant Cell Physiol. 44:655-660(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=16461379; DOI=10.1104/pp.105.076083;
RA   Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT   "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT   surprising site for differential accumulation of metabolic enzymes.";
RL   Plant Physiol. 140:984-997(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [9]
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).
RN   [10]
RP   METHYLATION AT LYS-387.
RX   PubMed=22547063; DOI=10.1074/jbc.m112.359976;
RA   Mininno M., Brugiere S., Pautre V., Gilgen A., Ma S., Ferro M., Tardif M.,
RA   Alban C., Ravanel S.;
RT   "Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as
RT   lysine-methylated proteins in plants.";
RL   J. Biol. Chem. 287:21034-21044(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: Plastid, chloroplast, plastoglobule
CC       {ECO:0000269|PubMed:16461379}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, and at low levels in rosettes
CC       leaves, cauline leaves, stems and flowers.
CC       {ECO:0000269|PubMed:22561114}.
CC   -!- INDUCTION: Down-regulated by oxidative stress (PubMed:12492832).
CC       Induced by fructose and sucrose (PubMed:22561114). Down-regulated by
CC       abiotic stresses (PubMed:22561114). {ECO:0000269|PubMed:12492832,
CC       ECO:0000269|PubMed:22561114}.
CC   -!- PTM: Can be trimethylated at Lys-387 by LSMT-L, but the trimethylation
CC       has no effect in vitro. {ECO:0000269|PubMed:22547063}.
CC   -!- PTM: S-glutathionylated. {ECO:0000269|PubMed:12881492}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC006200; AAD14543.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05406.1; -; Genomic_DNA.
DR   EMBL; AF325014; AAG40366.1; -; mRNA.
DR   EMBL; AY086203; AAM64281.1; -; mRNA.
DR   PIR; B84421; B84421.
DR   RefSeq; NP_178224.1; NM_126176.5.
DR   AlphaFoldDB; Q9ZU52; -.
DR   SMR; Q9ZU52; -.
DR   BioGRID; 47; 14.
DR   IntAct; Q9ZU52; 1.
DR   STRING; 3702.AT2G01140.1; -.
DR   iPTMnet; Q9ZU52; -.
DR   PaxDb; Q9ZU52; -.
DR   PRIDE; Q9ZU52; -.
DR   ProteomicsDB; 244956; -.
DR   EnsemblPlants; AT2G01140.1; AT2G01140.1; AT2G01140.
DR   GeneID; 814643; -.
DR   Gramene; AT2G01140.1; AT2G01140.1; AT2G01140.
DR   KEGG; ath:AT2G01140; -.
DR   Araport; AT2G01140; -.
DR   TAIR; locus:2038726; AT2G01140.
DR   eggNOG; KOG1557; Eukaryota.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   InParanoid; Q9ZU52; -.
DR   OMA; PWIGHRS; -.
DR   OrthoDB; 799973at2759; -.
DR   PhylomeDB; Q9ZU52; -.
DR   BioCyc; ARA:AT2G01140-MON; -.
DR   UniPathway; UPA00109; UER00183.
DR   PRO; PR:Q9ZU52; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZU52; baseline and differential.
DR   Genevisible; Q9ZU52; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0010287; C:plastoglobule; 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   PANTHER; PTHR11627; PTHR11627; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Glutathionylation; Glycolysis;
KW   Lyase; Methylation; Phosphoprotein; Plastid; Reference proteome;
KW   Schiff base; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..391
FT                   /note="Fructose-bisphosphate aldolase 3, chloroplastic"
FT                   /id="PRO_0000286528"
FT   ACT_SITE        218
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   ACT_SITE        260
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         302..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   SITE            391
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   MOD_RES         150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q944G9"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q944G9"
FT   MOD_RES         387
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:22547063"
SQ   SEQUENCE   391 AA;  42327 MW;  4512045C1C325D2A CRC64;
     MASASFVKPN TLSSPWIGQR SFAHTSASSS PPPRVSFAIR AGAYSDELVK TAKSIASPGR
     GILAIDESNA TCGKRLASIG LDNTEDNRQA YRQLLLTTPG LGDYISGSIL FEETLYQSTK
     DGKTFVDCLR DANIVPGIKV DKGLSPLAGS NEESWCQGLD GLASRSAEYY KQGARFAKWR
     TVVSVPCGPS ALAVKEAAWG LARYAAISQD NGLVPIVEPE ILLDGDHPIE RTLEVAEKVW
     SEVFFYLAQN NVMFEGILLK PSMVTPGAEH KNKASPETVA DFTLTMLKRR VPPAVPGIMF
     LSGGQSEAEA TLNLNAMNQS PNPWHVSFSY ARALQNSVLR TWQGKPEKIE ASQKALLVRA
     KANSLAQLGK YSAEGENEDA KKGMFVKGYT Y
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024