ID RBCMT_PEA Reviewed; 489 AA. AC Q43088; DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 119. DE RecName: Full=Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic; DE EC=2.1.1.127; DE AltName: Full=[Fructose-bisphosphate aldolase]-lysine N-methyltransferase; DE EC=2.1.1.259; DE AltName: Full=[Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase; DE Short=PsLSMT; DE Short=RuBisCO LSMT; DE Short=RuBisCO methyltransferase; DE Short=rbcMT; DE Flags: Precursor; GN Name=RBCMT; OS Pisum sativum (Garden pea) (Lathyrus oleraceus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Leaf; RX PubMed=7888616; DOI=10.1007/bf00020181; RA Klein R.R., Houtz R.L.; RT "Cloning and developmental expression of pea ribulose-1,5-bisphosphate RT carboxylase/oxygenase large subunit N-methyltransferase."; RL Plant Mol. Biol. 27:249-261(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 46-482 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF RP GLU-281, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12372303; DOI=10.1016/s0092-8674(02)01000-0; RA Trievel R.C., Beach B.M., Dirk L.M., Houtz R.L., Hurley J.H.; RT "Structure and catalytic mechanism of a SET domain protein RT methyltransferase."; RL Cell 111:91-103(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 46-482 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND SUBSTRATE. RX PubMed=12819771; DOI=10.1038/nsb946; RA Trievel R.C., Flynn E.M., Houtz R.L., Hurley J.H.; RT "Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco RT LSMT."; RL Nat. Struct. Biol. 10:545-552(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 49-482 IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND SUBSTRATE. RX PubMed=16682405; DOI=10.1074/jbc.m602257200; RA Couture J.F., Hauk G., Thompson M.J., Blackburn G.M., Trievel R.C.; RT "Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine RT methyltransferases."; RL J. Biol. Chem. 281:19280-19287(2006). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. 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: Methylates 'Lys-14' of the large subunit of RuBisCO. Can also CC use with lower efficiency chloroplastic fructose-bisphosphate aldolases CC and gamma-tocopherol methyltransferase as substrates, but not a CC cytosolic aldolase. {ECO:0000269|PubMed:22547063}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[ribulose-1,5-bisphosphate carboxylase] + 3 S- CC adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl- CC [ribulose-1,5-bisphosphate carboxylase] + 3 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:50996, Rhea:RHEA-COMP:12858, Rhea:RHEA- CC COMP:12859, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.127; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=12.9 uM for fructose-bisphosphate aldolase 2 CC {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; CC KM=14 uM for fructose-bisphosphate aldolase 3 CC {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; CC KM=32 uM for gamma-tocopherol methyltransferase CC {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; CC KM=4.5 uM for rubisco {ECO:0000269|PubMed:12372303, CC ECO:0000269|PubMed:22547063}; CC KM=6 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12372303, CC ECO:0000269|PubMed:22547063}; CC Vmax=19.5 nmol/min/mg enzyme with fructose-bisphosphate aldolase 2 as CC substrate {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; CC Vmax=9 nmol/min/mg enzyme with fructose-bisphosphate aldolase 3 as CC substrate {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; CC Vmax=1.7 nmol/min/mg enzyme with gamma-tocopherol methyltransferase CC as substrate {ECO:0000269|PubMed:12372303, CC ECO:0000269|PubMed:22547063}; CC Vmax=44.6 nmol/min/mg enzyme with rubisco as substrate CC {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; CC Vmax=56 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate CC {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063}; CC Note=kcat is 0.047 sec(-1) for S-adenosyl-L-methionine. kcat is 0.038 CC sec(-1) for rubisco.; CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12372303, CC ECO:0000269|PubMed:12819771, ECO:0000269|PubMed:16682405}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- TISSUE SPECIFICITY: Highly expressed in leaf. 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 --------------------------------------------------------------------------- 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; L34291; AAA69903.1; -; mRNA. DR PIR; S53005; S53005. DR PDB; 1MLV; X-ray; 2.60 A; A/B/C=46-482. DR PDB; 1OZV; X-ray; 2.65 A; A/B/C=46-482. DR PDB; 1P0Y; X-ray; 2.55 A; A/B/C=46-482. DR PDB; 2H21; X-ray; 2.45 A; A/B/C=49-482. DR PDB; 2H23; X-ray; 2.45 A; A/B/C=49-482. DR PDB; 2H2E; X-ray; 2.60 A; A/B/C=49-482. DR PDB; 2H2J; X-ray; 2.45 A; A/B/C=49-482. DR PDBsum; 1MLV; -. DR PDBsum; 1OZV; -. DR PDBsum; 1P0Y; -. DR PDBsum; 2H21; -. DR PDBsum; 2H23; -. DR PDBsum; 2H2E; -. DR PDBsum; 2H2J; -. DR AlphaFoldDB; Q43088; -. DR SMR; Q43088; -. DR DIP; DIP-48722N; -. DR IntAct; Q43088; 3. DR EnsemblPlants; Psat7g156240.1; Psat7g156240.1.cds1; Psat7g156240. DR Gramene; Psat7g156240.1; Psat7g156240.1.cds1; Psat7g156240. DR KEGG; ag:AAA69903; -. DR BRENDA; 2.1.1.127; 4872. DR BRENDA; 2.1.1.259; 4872. DR SABIO-RK; Q43088; -. DR EvolutionaryTrace; Q43088; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0030785; F:[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:InterPro. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. 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 SMART; SM00317; 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 3D-structure; Chloroplast; Direct protein sequencing; Methyltransferase; KW Plastid; S-adenosyl-L-methionine; Transferase; Transit peptide. FT TRANSIT 1..37 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 38..489 FT /note="Ribulose-1,5 bisphosphate carboxylase/oxygenase FT large subunit N-methyltransferase, chloroplastic" FT /id="PRO_0000022199" FT DOMAIN 64..288 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 80..82 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 222 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190, FT ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:12819771, FT ECO:0000269|PubMed:16682405" FT BINDING 222 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12819771, FT ECO:0000269|PubMed:16682405" FT BINDING 226 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12819771, FT ECO:0000269|PubMed:16682405" FT BINDING 239 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12819771, FT ECO:0000269|PubMed:16682405" FT BINDING 242..243 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 254 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12819771, FT ECO:0000269|PubMed:16682405" FT BINDING 287 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12819771, FT ECO:0000269|PubMed:16682405" FT BINDING 300 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12819771, FT ECO:0000269|PubMed:16682405" FT MUTAGEN 281 FT /note="E->Q: No effect on substrate affinity, but reduced FT catalytic activity." FT /evidence="ECO:0000269|PubMed:12372303" FT HELIX 52..63 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 66..70 FT /evidence="ECO:0007829|PDB:2H2E" FT STRAND 72..78 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 81..88 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 94..100 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:1P0Y" FT HELIX 124..137 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 144..147 FT /evidence="ECO:0007829|PDB:2H21" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 162..166 FT /evidence="ECO:0007829|PDB:2H21" FT TURN 167..170 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 172..194 FT /evidence="ECO:0007829|PDB:2H21" FT TURN 198..202 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 209..222 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 226..229 FT /evidence="ECO:0007829|PDB:1P0Y" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1P0Y" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:2H2J" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 268..275 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:2H23" FT HELIX 293..299 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 307..309 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 311..317 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 325..333 FT /evidence="ECO:0007829|PDB:2H21" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 339..346 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 355..363 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 366..372 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:2H21" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 380..386 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 390..408 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:1P0Y" FT HELIX 415..422 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 428..456 FT /evidence="ECO:0007829|PDB:2H21" FT TURN 457..460 FT /evidence="ECO:0007829|PDB:2H21" FT HELIX 464..469 FT /evidence="ECO:0007829|PDB:2H21" FT STRAND 474..476 FT /evidence="ECO:0007829|PDB:2H2E" FT HELIX 479..482 FT /evidence="ECO:0007829|PDB:2H21" SQ SEQUENCE 489 AA; 55110 MW; 72C53E37EE08AFC5 CRC64; MATIFSGGSV SPFLFHTNKG TSFTPKAPIL HLKRSFSAKS VASVGTEPSL SPAVQTFWKW LQEEGVITAK TPVKASVVTE GLGLVALKDI SRNDVILQVP KRLWINPDAV AASEIGRVCS ELKPWLSVIL FLIRERSRED SVWKHYFGIL PQETDSTIYW SEEELQELQG SQLLKTTVSV KEYVKNECLK LEQEIILPNK RLFPDPVTLD DFFWAFGILR SRAFSRLRNE NLVVVPMADL INHSAGVTTE DHAYEVKGAA GLFSWDYLFS LKSPLSVKAG EQVYIQYDLN KSNAELALDY GFIEPNENRH AYTLTLEISE SDPFFDDKLD VAESNGFAQT AYFDIFYNRT LPPGLLPYLR LVALGGTDAF LLESLFRDTI WGHLELSVSR DNEELLCKAV REACKSALAG YHTTIEQDRE LKEGNLDSRL AIAVGIREGE KMVLQQIDGI FEQKELELDQ LEYYQERRLK DLGLCGENGD ILGDLGKFF //