GenomeNet

Database: UniProt
Entry: Q9XI84
LinkDB: Q9XI84
Original site: Q9XI84 
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   13-FEB-2019, entry version 125.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RP   PHENOTYPE, 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.,
RA   Tardif M., Alban C., Ravanel S.;
RT   "Characterization of chloroplastic fructose 1,6-bisphosphate aldolases
RT   as lysine-methylated proteins in plants.";
RL   J. Biol. Chem. 287:21034-21044(2012).
CC   -!- FUNCTION: Protein-lysine methyltransferase methylating
CC       chloroplastic fructose 1,6-bisphosphate aldolases. Can also use
CC       with low efficiency gamma-tocopherol methyltransferase as
CC       substrate, but not a cytosolic aldolase. Able to interact with
CC       unmethylated Rubisco, but unlike in pea, the complex is
CC       catalytically unproductive. {ECO:0000269|PubMed:22547063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[fructose-bisphosphate aldolase]-L-lysine + 3 S-adenosyl-
CC         L-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-
CC         COMP:12862, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC         EC=2.1.1.259; 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
CC         2 as substrate {ECO:0000269|PubMed:22547063};
CC         Vmax=16.2 nmol/min/mg enzyme with fructose-bisphosphate aldolase
CC         3 as substrate {ECO:0000269|PubMed:22547063};
CC         Vmax=1.2 nmol/min/mg enzyme with gamma-tocopherol
CC         methyltransferase as substrate {ECO:0000269|PubMed:22547063};
CC   -!- INTERACTION:
CC       P46604:HAT22; NbExp=3; IntAct=EBI-15192835, EBI-4448318;
CC       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
CC       methyltransferase superfamily. Plant protein-lysine LSMT
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00916}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79410.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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   UniGene; At.41996; -.
DR   UniGene; At.41997; -.
DR   ProteinModelPortal; Q9XI84; -.
DR   SMR; Q9XI84; -.
DR   BioGrid; 23204; 58.
DR   IntAct; Q9XI84; 58.
DR   STRING; 3702.AT1G14030.1; -.
DR   PaxDb; Q9XI84; -.
DR   PRIDE; Q9XI84; -.
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; locus:2014764; AT1G14030.
DR   eggNOG; KOG1337; Eukaryota.
DR   eggNOG; ENOG410Y7DR; LUCA.
DR   HOGENOM; HOG000265866; -.
DR   InParanoid; Q9XI84; -.
DR   KO; K00592; -.
DR   OMA; CERADPN; -.
DR   OrthoDB; 489371at2759; -.
DR   PhylomeDB; Q9XI84; -.
DR   PRO; PR:Q9XI84; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q9XI84; AT.
DR   GO; GO:0009507; C:chloroplast; IDA: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:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:TAIR.
DR   Gene3D; 3.90.1420.10; -; 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   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF009328; RMT_SET; 1.
DR   SUPFAM; SSF81822; SSF81822; 1.
DR   PROSITE; PS51583; SAM_MT127; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Complete proteome; Methyltransferase; Plastid;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     57       Chloroplast. {ECO:0000255}.
FT   CHAIN        58    482       [Fructose-bisphosphate aldolase]-lysine
FT                                N-methyltransferase, chloroplastic.
FT                                /FTId=PRO_0000022198.
FT   DOMAIN       59    282       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION       75     77       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      237    238       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   BINDING     217    217       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     217    217       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING     221    221       Substrate. {ECO:0000250}.
FT   BINDING     234    234       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING     249    249       Substrate. {ECO:0000250}.
FT   BINDING     281    281       Substrate. {ECO:0000250}.
FT   BINDING     294    294       Substrate. {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
//
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