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RBCMT_ARATH
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   03-AUG-2022, entry version 141.
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; 58.
DR   IntAct; Q9XI84; 58.
DR   STRING; 3702.AT1G14030.1; -.
DR   PaxDb; Q9XI84; -.
DR   PRIDE; Q9XI84; -.
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; locus:2014764; AT1G14030.
DR   eggNOG; KOG1337; Eukaryota.
DR   HOGENOM; CLU_028149_1_0_1; -.
DR   InParanoid; Q9XI84; -.
DR   OMA; DFWMKIP; -.
DR   OrthoDB; 489371at2759; -.
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:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:TAIR.
DR   CDD; cd19179; SET_RBCMT; 1.
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   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR044431; SET_RBCMT.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF009328; RMT_SET; 1.
DR   SUPFAM; SSF81822; SSF81822; 1.
DR   SUPFAM; SSF82199; SSF82199; 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
 
 
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