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Database: UniProt
Entry: Q43088
LinkDB: Q43088
Original site: Q43088 
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   05-DEC-2018, entry version 103.
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).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   50 kb inversion clade; NPAAA clade; Hologalegina; IRL clade; Fabeae;
OC   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
RT   Rubisco 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
RT   lysine 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.,
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: Methylates 'Lys-14' of the large subunit of RuBisCO. Can
CC       also use with lower efficiency chloroplastic fructose-bisphosphate
CC       aldolases and gamma-tocopherol methyltransferase as substrates,
CC       but not a cytosolic aldolase. {ECO:0000269|PubMed:22547063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ribulose-1,5-bisphosphate carboxylase]-L-lysine + 3 S-
CC         adenosyl-L-methionine = [ribulose-1,5-bisphosphate carboxylase]-
CC         N(6),N(6),N(6)-trimethyl-L-lysine + 3 H(+) + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:50996, Rhea:RHEA-COMP:12858,
CC         Rhea:RHEA-COMP:12859, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC         EC=2.1.1.127;
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;
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=14.0 uM for fructose-bisphosphate aldolase 3
CC         {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063};
CC         KM=32.0 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
CC         {ECO:0000269|PubMed:12372303, ECO:0000269|PubMed:22547063};
CC         Vmax=19.5 nmol/min/mg enzyme with fructose-bisphosphate aldolase
CC         2 as substrate {ECO:0000269|PubMed:12372303,
CC         ECO:0000269|PubMed:22547063};
CC         Vmax=9.0 nmol/min/mg enzyme with fructose-bisphosphate aldolase
CC         3 as substrate {ECO:0000269|PubMed:12372303,
CC         ECO:0000269|PubMed:22547063};
CC         Vmax=1.7 nmol/min/mg enzyme with gamma-tocopherol
CC         methyltransferase 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
CC         substrate {ECO:0000269|PubMed:12372303,
CC         ECO:0000269|PubMed:22547063};
CC         Note=Kcat is 0.047 sec(-1) for S-adenosyl-L-methionine. Kcat is
CC         0.038 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
CC       methyltransferase superfamily. Plant protein-lysine LSMT
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00916}.
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   ProteinModelPortal; Q43088; -.
DR   SMR; Q43088; -.
DR   DIP; DIP-48722N; -.
DR   IntAct; Q43088; 3.
DR   KEGG; ag:AAA69903; -.
DR   KO; K00592; -.
DR   BRENDA; 2.1.1.127; 4872.
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   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   SMART; SM00317; 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   3D-structure; Chloroplast; Direct protein sequencing;
KW   Methyltransferase; Plastid; S-adenosyl-L-methionine; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     37       Chloroplast. {ECO:0000255}.
FT   CHAIN        38    489       Ribulose-1,5 bisphosphate
FT                                carboxylase/oxygenase large subunit N-
FT                                methyltransferase, chloroplastic.
FT                                /FTId=PRO_0000022199.
FT   DOMAIN       64    288       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION       80     82       S-adenosyl-L-methionine binding.
FT   REGION      242    243       S-adenosyl-L-methionine binding.
FT   BINDING     222    222       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|PubMed:12372303,
FT                                ECO:0000269|PubMed:12819771,
FT                                ECO:0000269|PubMed:16682405}.
FT   BINDING     222    222       Substrate; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:12819771,
FT                                ECO:0000269|PubMed:16682405}.
FT   BINDING     226    226       Substrate. {ECO:0000269|PubMed:12819771,
FT                                ECO:0000269|PubMed:16682405}.
FT   BINDING     239    239       Substrate; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:12819771,
FT                                ECO:0000269|PubMed:16682405}.
FT   BINDING     254    254       Substrate. {ECO:0000269|PubMed:12819771,
FT                                ECO:0000269|PubMed:16682405}.
FT   BINDING     287    287       Substrate. {ECO:0000269|PubMed:12819771,
FT                                ECO:0000269|PubMed:16682405}.
FT   BINDING     300    300       Substrate. {ECO:0000269|PubMed:12819771,
FT                                ECO:0000269|PubMed:16682405}.
FT   MUTAGEN     281    281       E->Q: No effect on substrate affinity,
FT                                but reduced catalytic activity.
FT                                {ECO:0000269|PubMed:12372303}.
FT   HELIX        52     63       {ECO:0000244|PDB:2H21}.
FT   STRAND       66     70       {ECO:0000244|PDB:2H2E}.
FT   STRAND       72     78       {ECO:0000244|PDB:2H21}.
FT   STRAND       81     88       {ECO:0000244|PDB:2H21}.
FT   STRAND       94    100       {ECO:0000244|PDB:2H21}.
FT   HELIX       101    103       {ECO:0000244|PDB:2H21}.
FT   HELIX       107    110       {ECO:0000244|PDB:2H21}.
FT   HELIX       116    119       {ECO:0000244|PDB:2H21}.
FT   STRAND      120    122       {ECO:0000244|PDB:1P0Y}.
FT   HELIX       124    137       {ECO:0000244|PDB:2H21}.
FT   HELIX       144    147       {ECO:0000244|PDB:2H21}.
FT   TURN        157    159       {ECO:0000244|PDB:2H21}.
FT   HELIX       162    166       {ECO:0000244|PDB:2H21}.
FT   TURN        167    170       {ECO:0000244|PDB:2H21}.
FT   HELIX       172    194       {ECO:0000244|PDB:2H21}.
FT   TURN        198    202       {ECO:0000244|PDB:2H21}.
FT   HELIX       209    222       {ECO:0000244|PDB:2H21}.
FT   STRAND      226    229       {ECO:0000244|PDB:1P0Y}.
FT   STRAND      231    233       {ECO:0000244|PDB:1P0Y}.
FT   HELIX       238    240       {ECO:0000244|PDB:2H2J}.
FT   STRAND      253    255       {ECO:0000244|PDB:2H21}.
FT   HELIX       258    260       {ECO:0000244|PDB:2H21}.
FT   HELIX       264    266       {ECO:0000244|PDB:2H21}.
FT   STRAND      268    275       {ECO:0000244|PDB:2H21}.
FT   STRAND      281    285       {ECO:0000244|PDB:2H23}.
FT   HELIX       293    299       {ECO:0000244|PDB:2H21}.
FT   HELIX       307    309       {ECO:0000244|PDB:2H21}.
FT   STRAND      311    317       {ECO:0000244|PDB:2H21}.
FT   HELIX       325    333       {ECO:0000244|PDB:2H21}.
FT   TURN        334    336       {ECO:0000244|PDB:2H21}.
FT   STRAND      339    346       {ECO:0000244|PDB:2H21}.
FT   HELIX       355    363       {ECO:0000244|PDB:2H21}.
FT   HELIX       366    372       {ECO:0000244|PDB:2H21}.
FT   HELIX       374    376       {ECO:0000244|PDB:2H21}.
FT   TURN        377    379       {ECO:0000244|PDB:2H21}.
FT   HELIX       380    386       {ECO:0000244|PDB:2H21}.
FT   HELIX       390    408       {ECO:0000244|PDB:2H21}.
FT   STRAND      411    413       {ECO:0000244|PDB:1P0Y}.
FT   HELIX       415    422       {ECO:0000244|PDB:2H21}.
FT   HELIX       428    456       {ECO:0000244|PDB:2H21}.
FT   TURN        457    460       {ECO:0000244|PDB:2H21}.
FT   HELIX       464    469       {ECO:0000244|PDB:2H21}.
FT   STRAND      474    476       {ECO:0000244|PDB:2H2E}.
FT   HELIX       479    482       {ECO:0000244|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
//
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