位置:首页 > 蛋白库 > ALFP1_ARATH
ALFP1_ARATH
ID   ALFP1_ARATH             Reviewed;         399 AA.
AC   Q9SJU4; Q2V473; Q93WF5; Q94C97;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Fructose-bisphosphate aldolase 1, chloroplastic {ECO:0000305};
DE            Short=AtFBA1 {ECO:0000303|PubMed:22561114};
DE            EC=4.1.2.13 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=FBA1 {ECO:0000303|PubMed:22561114}; OrderedLocusNames=At2g21330;
GN   ORFNames=F3K23.9;
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   PROTEIN SEQUENCE OF 49-60, AND SUBCELLULAR LOCATION.
RX   PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA   Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA   Kieselbach T.;
RT   "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL   J. Biol. Chem. 277:8354-8365(2002).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND GLUTATHIONYLATION.
RX   PubMed=15734904; DOI=10.1104/pp.104.058719;
RA   Lindermayr C., Saalbach G., Durner J.;
RT   "Proteomic identification of S-nitrosylated proteins in Arabidopsis.";
RL   Plant Physiol. 137:921-930(2005).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Col-2;
RX   PubMed=16414959; DOI=10.1074/jbc.m511939200;
RA   Vidi P.-A., Kanwischer M., Baginsky S., Austin J.R., Csucs G., Doermann P.,
RA   Kessler F., Brehelin C.;
RT   "Tocopherol cyclase (VTE1) localization and vitamin E accumulation in
RT   chloroplast plastoglobule lipoprotein particles.";
RL   J. Biol. Chem. 281:11225-11234(2006).
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   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   [9]
RP   METHYLATION AT LYS-395.
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:11719511, ECO:0000269|PubMed:16414959,
CC       ECO:0000269|PubMed:16461379}. Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:16414959}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9SJU4-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Highly expressed in rosettes leaves and cauline
CC       leaves. {ECO:0000269|PubMed:22561114}.
CC   -!- INDUCTION: By sucrose (PubMed:22561114). Induced by drought stress
CC       (PubMed:22561114). {ECO:0000269|PubMed:22561114}.
CC   -!- PTM: Can be trimethylated at Lys-395 by LSMT-L, but the trimethylation
CC       has no effect in vitro on the kinetic properties of the enzyme.
CC       {ECO:0000269|PubMed:22547063}.
CC   -!- PTM: S-glutathionylated. {ECO:0000269|PubMed:15734904}.
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; AC006841; AAD23681.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07160.1; -; Genomic_DNA.
DR   EMBL; AF419589; AAL31921.1; -; mRNA.
DR   EMBL; AF428408; AAL16176.1; -; mRNA.
DR   EMBL; AY035043; AAK59548.1; -; mRNA.
DR   EMBL; AY049282; AAK83624.1; -; mRNA.
DR   EMBL; AY049286; AAK83628.1; -; mRNA.
DR   EMBL; AY062582; AAL32660.1; -; mRNA.
DR   EMBL; AY090291; AAL90952.1; -; mRNA.
DR   EMBL; AY128380; AAM91583.1; -; mRNA.
DR   EMBL; AY128784; AAM91184.1; -; mRNA.
DR   EMBL; AY142633; AAN13091.1; -; mRNA.
DR   EMBL; BT000106; AAN15425.1; -; mRNA.
DR   EMBL; BT002415; AAO00775.1; -; mRNA.
DR   PIR; A84600; A84600.
DR   RefSeq; NP_565508.1; NM_127705.4. [Q9SJU4-1]
DR   AlphaFoldDB; Q9SJU4; -.
DR   SMR; Q9SJU4; -.
DR   BioGRID; 2025; 3.
DR   STRING; 3702.AT2G21330.1; -.
DR   iPTMnet; Q9SJU4; -.
DR   World-2DPAGE; 0003:Q9SJU4; -.
DR   PaxDb; Q9SJU4; -.
DR   PRIDE; Q9SJU4; -.
DR   ProteomicsDB; 245045; -. [Q9SJU4-1]
DR   EnsemblPlants; AT2G21330.1; AT2G21330.1; AT2G21330. [Q9SJU4-1]
DR   GeneID; 816672; -.
DR   Gramene; AT2G21330.1; AT2G21330.1; AT2G21330. [Q9SJU4-1]
DR   KEGG; ath:AT2G21330; -.
DR   Araport; AT2G21330; -.
DR   TAIR; locus:2050049; AT2G21330.
DR   eggNOG; KOG1557; Eukaryota.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   InParanoid; Q9SJU4; -.
DR   OMA; EVASMVW; -.
DR   PhylomeDB; Q9SJU4; -.
DR   BioCyc; ARA:AT2G21330-MON; -.
DR   UniPathway; UPA00109; UER00183.
DR   PRO; PR:Q9SJU4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJU4; baseline and differential.
DR   Genevisible; Q9SJU4; AT.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; 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:0022626; C:cytosolic ribosome; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0031977; C:thylakoid lumen; 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   Alternative splicing; Chloroplast; Direct protein sequencing;
KW   Glutathionylation; Glycolysis; Lyase; Methylation; Phosphoprotein; Plastid;
KW   Reference proteome; Schiff base; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:11719511"
FT   CHAIN           49..399
FT                   /note="Fructose-bisphosphate aldolase 1, chloroplastic"
FT                   /id="PRO_0000286526"
FT   ACT_SITE        226
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   ACT_SITE        268
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   BINDING         310..312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   SITE            399
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q944G9"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q944G9"
FT   MOD_RES         395
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:22547063"
FT   CONFLICT        236
FT                   /note="G -> S (in Ref. 3; AAK59548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315
FT                   /note="E -> G (in Ref. 3; AAK59548)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   399 AA;  42931 MW;  26CC71FA3C571B53 CRC64;
     MASSTATMLK ASPVKSDWVK GQSLLLRQPS SVSAIRSHVA PSALTVRAAS AYADELVKTA
     KTIASPGHGI MAMDESNATC GKRLASIGLE NTEANRQAYR TLLVSAPGLG QYISGAILFE
     ETLYQSTTDG KKMVDVLVEQ NIVPGIKVDK GLVPLVGSYD ESWCQGLDGL ASRTAAYYQQ
     GARFAKWRTV VSIPNGPSAL AVKEAAWGLA RYAAISQDSG LVPIVEPEIM LDGEHGIDRT
     YDVAEKVWAE VFFYLAQNNV MFEGILLKPS MVTPGAEATD RATPEQVASY TLKLLRNRIP
     PAVPGIMFLS GGQSELEATL NLNAMNQAPN PWHVSFSYAR ALQNTCLKTW GGKEENVKAA
     QDILLARAKA NSLAQLGKYT GEGESEEAKE GMFVKGYTY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024