F26_ARATH
ID F26_ARATH Reviewed; 744 AA.
AC Q9MB58; Q8L7N6; Q9LL39; Q9LMK3; Q9SP17;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase;
DE Short=6PF-2-K/Fru-2,6-P2ase;
DE Short=AtF2KP;
DE Short=PFK/FBPase;
DE Includes:
DE RecName: Full=6-phosphofructo-2-kinase;
DE EC=2.7.1.105;
DE Includes:
DE RecName: Full=Fructose-2,6-bisphosphatase;
DE EC=3.1.3.46;
GN Name=FKFBP; Synonyms=F2KP; OrderedLocusNames=At1g07110; ORFNames=F10K1.19;
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 / MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10899575; DOI=10.1016/s0167-4781(00)00134-2;
RA Villadsen D., Rung J.H., Draborg H., Nielsen T.H.;
RT "Structure and heterologous expression of a gene encoding fructose-6-
RT phosphate,2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1492:406-413(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Furumoto T., Ito M., Akira W.;
RT "cDNA cloning of the gene for Fructose-6-phosphate,2-kinase/Fructose-2,6-
RT bisphosphatase from Arabidopsis.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-744.
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 [6]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11672433; DOI=10.1042/0264-6021:3590591;
RA Villadsen D., Nielsen T.H.;
RT "N-terminal truncation affects the kinetics and structure of fructose-6-
RT phosphate 2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana.";
RL Biochem. J. 359:591-597(2001).
RN [7]
RP FUNCTION IN CARBON PARTITIONING.
RX PubMed=11402203; DOI=10.1104/pp.126.2.750;
RA Draborg H., Villadsen D., Nielsen T.H.;
RT "Transgenic Arabidopsis plants with decreased activity of fructose-6-
RT phosphate,2-kinase/fructose-2,6-bisphosphatase have altered carbon
RT partitioning.";
RL Plant Physiol. 126:750-758(2001).
RN [8]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=12912986; DOI=10.1074/jbc.m307321200;
RA Boisson B., Giglione C., Meinnel T.;
RT "Unexpected protein families including cell defense components feature in
RT the N-myristoylome of a higher eukaryote.";
RL J. Biol. Chem. 278:43418-43429(2003).
RN [9]
RP FUNCTION, PHOSPHORYLATION AT SER-220 AND SER-303 BY CPK3, AND INTERACTION
RP WITH 14-3-3 PROTEINS.
RX PubMed=14871307; DOI=10.1111/j.1365-313x.2003.01992.x;
RA Kulma A., Villadsen D., Campbell D.G., Meek S.E.M., Harthill J.E.,
RA Nielsen T.H., MacKintosh C.;
RT "Phosphorylation and 14-3-3 binding of Arabidopsis 6-phosphofructo-2-
RT kinase/fructose-2,6-bisphosphatase.";
RL Plant J. 37:654-667(2004).
RN [10]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-276 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC Regulates carbon partitioning between sucrose versus starch during the
CC diurnal cycle. {ECO:0000269|PubMed:10899575,
CC ECO:0000269|PubMed:11402203, ECO:0000269|PubMed:14871307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46;
CC Evidence={ECO:0000269|PubMed:11672433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579,
CC ChEBI:CHEBI:456216; EC=2.7.1.105;
CC Evidence={ECO:0000269|PubMed:11672433};
CC -!- ACTIVITY REGULATION: 6-phosphofructo-2-kinase activity is activated by
CC pyruvate. 6-phosphofructo-2-kinase activity is inhibited by PPi,
CC phosphoenolpyruvate and 2-phosphoglycerate. Fructose-2,6-bisphosphatase
CC activity is inhibited by pyruvate, fructose 1,6-bisphosphate and 6-
CC phosphogluconate. {ECO:0000269|PubMed:11672433}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for fructose-6-phosphate for the 6-phosphofructo-2-kinase
CC activity (at pH 6.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:11672433};
CC KM=0.19 mM for ATP for the 6-phosphofructo-2-kinase activity (at pH
CC 6.0 and 25 degrees Celsius) {ECO:0000269|PubMed:11672433};
CC KM=0.028 mM for fructose-2,6-bisphosphate for the fructose-2,6-
CC bisphosphatase activity (at pH 6.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:11672433};
CC Vmax=180 nmol/min/mg enzyme with fructose-6-phosphate as substrate
CC for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:11672433};
CC Vmax=270 nmol/min/mg enzyme with fructose-2,6-bisphosphate as
CC substrate for the fructose-2,6-bisphosphatase activity (at pH 6.0 and
CC 25 degrees Celsius) {ECO:0000269|PubMed:11672433};
CC Temperature dependence:
CC Inactivated by mild heat treatment (42 degrees Celsius during 10
CC minutes). {ECO:0000269|PubMed:11672433};
CC -!- SUBUNIT: Interacts with 14-3-3 proteins; these interactions may
CC regulate both nitrate assimilation and sucrose/starch partitioning in
CC leaves during the diurnal cycle. {ECO:0000269|PubMed:14871307}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18433157}; Lipid-
CC anchor {ECO:0000269|PubMed:18433157}; Cytoplasmic side
CC {ECO:0000269|PubMed:18433157}. Cytoplasm {ECO:0000269|PubMed:18433157}.
CC -!- PTM: Phosphorylation at Ser-220 and Ser-303 by CPK3 promotes 14-3-3
CC proteins binding. {ECO:0000269|PubMed:14871307}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76986.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF82210.1; Type=Erroneous gene model prediction; Evidence={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; AF190739; AAF04293.2; -; mRNA.
DR EMBL; AF242859; AAF76986.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AB035288; BAA96353.1; -; mRNA.
DR EMBL; AC067971; AAF82210.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28077.1; -; Genomic_DNA.
DR EMBL; AY128346; AAM91549.1; -; mRNA.
DR PIR; H86205; H86205.
DR RefSeq; NP_172191.1; NM_100584.5.
DR AlphaFoldDB; Q9MB58; -.
DR SMR; Q9MB58; -.
DR STRING; 3702.AT1G07110.1; -.
DR iPTMnet; Q9MB58; -.
DR PaxDb; Q9MB58; -.
DR PRIDE; Q9MB58; -.
DR ProMEX; Q9MB58; -.
DR ProteomicsDB; 222358; -.
DR EnsemblPlants; AT1G07110.1; AT1G07110.1; AT1G07110.
DR GeneID; 837221; -.
DR Gramene; AT1G07110.1; AT1G07110.1; AT1G07110.
DR KEGG; ath:AT1G07110; -.
DR Araport; AT1G07110; -.
DR TAIR; locus:2007367; AT1G07110.
DR eggNOG; KOG0234; Eukaryota.
DR HOGENOM; CLU_025830_0_0_1; -.
DR InParanoid; Q9MB58; -.
DR OMA; YQENLRP; -.
DR OrthoDB; 198523at2759; -.
DR PhylomeDB; Q9MB58; -.
DR BioCyc; ARA:AT1G07110-MON; -.
DR BRENDA; 2.7.1.105; 399.
DR BRENDA; 3.1.3.46; 399.
DR PRO; PR:Q9MB58; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MB58; baseline and differential.
DR Genevisible; Q9MB58; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IBA:GO_Central.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006000; P:fructose metabolic process; IDA:UniProtKB.
DR GO; GO:0043609; P:regulation of carbon utilization; IMP:UniProtKB.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR10606; PTHR10606; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM01065; CBM_2; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Cytoplasm; Hydrolase; Kinase;
KW Lipoprotein; Membrane; Multifunctional enzyme; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..744
FT /note="6-phosphofructo-2-kinase/fructose-2,6-
FT bisphosphatase"
FT /id="PRO_0000415319"
FT DOMAIN 17..122
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..549
FT /note="6-phosphofructo-2-kinase"
FT REGION 550..744
FT /note="Fructose-2,6-bisphosphatase"
FT COMPBIAS 213..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /evidence="ECO:0000255"
FT ACT_SITE 460
FT /evidence="ECO:0000255"
FT ACT_SITE 558
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT ACT_SITE 630
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 349..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 382
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 406
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 433
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 439
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 469..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 496
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 500
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 557
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 564
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 570
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 641
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 652..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 655
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 659
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 670
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 697..701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 697
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 701
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT SITE 557
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 564
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT SITE 696
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT MOD_RES 220
FT /note="Phosphoserine; by CPK3"
FT /evidence="ECO:0000269|PubMed:14871307,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 303
FT /note="Phosphoserine; by CPK3"
FT /evidence="ECO:0000269|PubMed:14871307,
FT ECO:0007744|PubMed:18433157"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12912986"
FT CONFLICT 629
FT /note="D -> A (in Ref. 1; AAF04293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 82559 MW; 61EA630DFA01F38A CRC64;
MGSGASKNTE EDDDGSNGGG GQLYVSLKME NSKVEGELTP HVYGSLPLIG SWDPSKALPM
QRESALMSEL SFVVPPDHET LDFKFLLKPK NRNTPCIVEE GENRLLTGGS LQGDARLALF
RLEGDVIVEF RVFINADRVS PIDLATSWRA YRENLQPSTV RGIPDVSINP DPKSAECPLE
SLELDLAHYE VPAPAPSANS YLVYAADNAE NPRSLSASGS FRNDSTPKAA QRNSEDSGVT
VDGSPSAKEM TIVVPDSSNI YSAFGEAESK SVETLSPFQQ KDGQKGLFVD RGVGSPRLVK
SLSASSFLID TKQIKNSMPA AAGAVAAAAV ADQMLGPKED RHLAIVLVGL PARGKTFTAA
KLTRYLRWLG HDTKHFNVGK YRRLKHGVNM SADFFRADNP EGVEARTEVA ALAMEDMIAW
MQEGGQVGIF DATNSTRVRR NMLMKMAEGK CKIIFLETLC NDERIIERNI RLKIQQSPDY
SEEMDFEAGV RDFRDRLANY EKVYEPVEEG SYIKMIDMVS GNGGQIQVNN ISGYLPGRIV
FFLVNTHLTP RPILLTRHGE SMDNVRGRIG GDSVISDSGK LYAKKLASFV EKRLKSEKAA
SIWTSTLQRT NLTASSIVGF PKVQWRALDE INAGVCDGMT YEEVKKNMPE EYESRKKDKL
RYRYPRGESY LDVIQRLEPV IIELERQRAP VVVISHQAVL RALYAYFADR PLKEIPQIEM
PLHTIIEIQM GVSGVQEKRY KLMD
