ID RBCMT_ARATH Reviewed; 482 AA.
AC Q9XI84; Q9LMF5;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=[Fructose-bisphosphate aldolase]-lysine N-methyltransferase, chloroplastic;
DE EC=2.1.1.259;
DE AltName: Full=Aldolases N-methyltransferase;
DE AltName: Full=[Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase-like;
DE Short=AtLSMT-L;
DE Short=LSMT-like enzyme;
DE Flags: Precursor;
GN Name=LSMT-L; Synonyms=RBCMT; OrderedLocusNames=At1g14030;
GN ORFNames=F16A14.25, F7A19.12;
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=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 [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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
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: Protein-lysine methyltransferase methylating chloroplastic
CC fructose 1,6-bisphosphate aldolases. Can also use with low efficiency
CC gamma-tocopherol methyltransferase as substrate, but not a cytosolic
CC aldolase. Able to interact with unmethylated Rubisco, but unlike in
CC pea, the complex is catalytically unproductive.
CC {ECO:0000269|PubMed:22547063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[fructose-bisphosphate aldolase]-L-lysine + 3 S-adenosyl-L-
CC methionine = [fructose-bisphosphate aldolase]-N(6),N(6),N(6)-
CC trimethyl-L-lysine + 3 H(+) + 3 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51000, Rhea:RHEA-COMP:12861, Rhea:RHEA-COMP:12862,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.259;
CC Evidence={ECO:0000269|PubMed:22547063};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.8 uM for fructose-bisphosphate aldolase 2
CC {ECO:0000269|PubMed:22547063};
CC KM=14.8 uM for fructose-bisphosphate aldolase 3
CC {ECO:0000269|PubMed:22547063};
CC KM=31.4 uM for gamma-tocopherol methyltransferase
CC {ECO:0000269|PubMed:22547063};
CC Vmax=17.0 nmol/min/mg enzyme with fructose-bisphosphate aldolase 2 as
CC substrate {ECO:0000269|PubMed:22547063};
CC Vmax=16.2 nmol/min/mg enzyme with fructose-bisphosphate aldolase 3 as
CC substrate {ECO:0000269|PubMed:22547063};
CC Vmax=1.2 nmol/min/mg enzyme with gamma-tocopherol methyltransferase
CC as substrate {ECO:0000269|PubMed:22547063};
CC -!- INTERACTION:
CC Q9XI84; P46604: HAT22; NbExp=3; IntAct=EBI-15192835, EBI-4448318;
CC Q9XI84; Q38824: IAA6; NbExp=3; IntAct=EBI-15192835, EBI-1554124;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:22547063}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:22547063}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Plant protein-lysine LSMT methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00916}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79410.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007576; AAD39289.1; -; Genomic_DNA.
DR EMBL; AC068197; AAF79410.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29100.1; -; Genomic_DNA.
DR EMBL; BT005791; AAO64193.1; -; mRNA.
DR PIR; F86273; F86273.
DR RefSeq; NP_172856.1; NM_101269.2.
DR AlphaFoldDB; Q9XI84; -.
DR SMR; Q9XI84; -.
DR BioGRID; 23204; 59.
DR IntAct; Q9XI84; 58.
DR STRING; 3702.Q9XI84; -.
DR PaxDb; 3702-AT1G14030-1; -.
DR ProteomicsDB; 225906; -.
DR EnsemblPlants; AT1G14030.1; AT1G14030.1; AT1G14030.
DR GeneID; 837964; -.
DR Gramene; AT1G14030.1; AT1G14030.1; AT1G14030.
DR KEGG; ath:AT1G14030; -.
DR Araport; AT1G14030; -.
DR TAIR; AT1G14030; LSMT-L.
DR eggNOG; KOG1337; Eukaryota.
DR HOGENOM; CLU_028149_1_0_1; -.
DR InParanoid; Q9XI84; -.
DR OMA; DFWMKIP; -.
DR OrthoDB; 51002at2759; -.
DR PhylomeDB; Q9XI84; -.
DR BRENDA; 2.1.1.259; 399.
DR PRO; PR:Q9XI84; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI84; baseline and differential.
DR Genevisible; Q9XI84; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0030785; F:[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:TAIR.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:TAIR.
DR CDD; cd19179; SET_RBCMT; 1.
DR Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1.
DR Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 1.
DR InterPro; IPR011192; Rubisco_LSMT_MeTrfase_plant.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044431; SET_RBCMT.
DR PANTHER; PTHR13271:SF113; [FRUCTOSE-BISPHOSPHATE ALDOLASE]-LYSINE N-METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR PIRSF; PIRSF009328; RMT_SET; 1.
DR SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51583; SAM_MT127; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Methyltransferase; Plastid; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..482
FT /note="[Fructose-bisphosphate aldolase]-lysine N-
FT methyltransferase, chloroplastic"
FT /id="PRO_0000022198"
FT DOMAIN 59..282
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 75..77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237..238
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 482 AA; 54612 MW; 9E93472B5B14EFC6 CRC64;
MSASVAVVSG FLRIPSIQKS QNPSFLFSRP KKSLVRPISA SSSELPENVR NFWKWLRDQG
VVSGKSVAEP AVVPEGLGLV ARRDIGRNEV VLEIPKRLWI NPETVTASKI GPLCGGLKPW
VSVALFLIRE KYEEESSWRV YLDMLPQSTD STVFWSEEEL AELKGTQLLS TTLGVKEYVE
NEFLKLEQEI LLPNKDLFSS RITLDDFIWA FGILKSRAFS RLRGQNLVLI PLADLINHNP
AIKTEDYAYE IKGAGLFSRD LLFSLKSPVY VKAGEQVYIQ YDLNKSNAEL ALDYGFVESN
PKRNSYTLTI EIPESDPFFG DKLDIAESNK MGETGYFDIV DGQTLPAGML QYLRLVALGG
PDAFLLESIF NNTIWGHLEL PVSRTNEELI CRVVRDACKS ALSGFDTTIE EDEKLLDKGK
LEPRLEMALK IRIGEKRVLQ QIDQIFKDRE LELDILEYYQ ERRLKDLGLV GEQGDIIFWE
TK
//
