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Q43088 (RBCMT_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic
EC=2.1.1.127
Alternative name(s):
[Fructose-bisphosphate aldolase]-lysine N-methyltransferase
EC=2.1.1.259
[Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
Short name=PsLSMT
Short name=RuBisCO LSMT
Short name=RuBisCO methyltransferase
Short name=rbcMT
Gene names
Name:RBCMT
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Methylates 'Lys-14' of the large subunit of RuBisCO. Can also use with lower efficiency chloroplastic fructose-bisphosphate aldolases and gamma-tocopherol methyltransferase as substrates, but not a cytosolic aldolase. Ref.5

Catalytic activity

3 S-adenosyl-L-methionine + [ribulose-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-bisphosphate carboxylase]-N6,N6,N(6)-trimethyl-L-lysine. Ref.2 Ref.5

3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine = 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N(6)-trimethyl-L-lysine. Ref.2 Ref.5

Subunit structure

Homotrimer. Ref.2

Subcellular location

Plastid › chloroplast.

Tissue specificity

Highly expressed in leaf.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Rubisco methyltransferase family.

Contains 1 SET domain.

Biophysicochemical properties

Kinetic parameters:

Kcat is 0.047 sec(-1) for S-adenosyl-L-methionine. Kcat is 0.038 sec(-1) for rubisco.

KM=12.9 µM for fructose-bisphosphate aldolase 2 Ref.2 Ref.5

KM=14.0 µM for fructose-bisphosphate aldolase 3

KM=32.0 µM for gamma-tocopherol methyltransferase

KM=4.5 µM for rubisco

KM=6 µM for S-adenosyl-L-methionine

Vmax=19.5 nmol/min/mg enzyme with fructose-bisphosphate aldolase 2 as substrate

Vmax=9.0 nmol/min/mg enzyme with fructose-bisphosphate aldolase 3 as substrate

Vmax=1.7 nmol/min/mg enzyme with gamma-tocopherol methyltransferase as substrate

Vmax=44.6 nmol/min/mg enzyme with rubisco as substrate

Vmax=56 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Chloroplast Potential
Chain38 – 489452Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic
PRO_0000022199

Regions

Domain71 – 294224SET
Region80 – 823S-adenosyl-L-methionine binding
Region242 – 2432S-adenosyl-L-methionine binding

Sites

Binding site2221S-adenosyl-L-methionine
Binding site2221Substrate; via carbonyl oxygen
Binding site2261Substrate
Binding site2391Substrate; via carbonyl oxygen
Binding site2541Substrate
Binding site2871Substrate
Binding site3001Substrate

Experimental info

Mutagenesis2811E → Q: No effect on substrate affinity, but reduced catalytic activity. Ref.2

Secondary structure

1 .............................................................................. 489
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q43088 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 72C53E37EE08AFC5

FASTA48955,110
        10         20         30         40         50         60 
MATIFSGGSV SPFLFHTNKG TSFTPKAPIL HLKRSFSAKS VASVGTEPSL SPAVQTFWKW 

        70         80         90        100        110        120 
LQEEGVITAK TPVKASVVTE GLGLVALKDI SRNDVILQVP KRLWINPDAV AASEIGRVCS 

       130        140        150        160        170        180 
ELKPWLSVIL FLIRERSRED SVWKHYFGIL PQETDSTIYW SEEELQELQG SQLLKTTVSV 

       190        200        210        220        230        240 
KEYVKNECLK LEQEIILPNK RLFPDPVTLD DFFWAFGILR SRAFSRLRNE NLVVVPMADL 

       250        260        270        280        290        300 
INHSAGVTTE DHAYEVKGAA GLFSWDYLFS LKSPLSVKAG EQVYIQYDLN KSNAELALDY 

       310        320        330        340        350        360 
GFIEPNENRH AYTLTLEISE SDPFFDDKLD VAESNGFAQT AYFDIFYNRT LPPGLLPYLR 

       370        380        390        400        410        420 
LVALGGTDAF LLESLFRDTI WGHLELSVSR DNEELLCKAV REACKSALAG YHTTIEQDRE 

       430        440        450        460        470        480 
LKEGNLDSRL AIAVGIREGE KMVLQQIDGI FEQKELELDQ LEYYQERRLK DLGLCGENGD 


ILGDLGKFF

« Hide

References

[1]"Cloning and developmental expression of pea ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit N-methyltransferase."
Klein R.R., Houtz R.L.
Plant Mol. Biol. 27:249-261(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Leaf.
[2]"Structure and catalytic mechanism of a SET domain protein methyltransferase."
Trievel R.C., Beach B.M., Dirk L.M., Houtz R.L., Hurley J.H.
Cell 111:91-103(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 46-482 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF GLU-281, BIOPHYSICOCHEMICAL PROPERTIES.
[3]"Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT."
Trievel R.C., Flynn E.M., Houtz R.L., Hurley J.H.
Nat. Struct. Biol. 10:545-552(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 46-482 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND SUBSTRATE.
[4]"Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases."
Couture J.F., Hauk G., Thompson M.J., Blackburn G.M., Trievel R.C.
J. Biol. Chem. 281:19280-19287(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 49-482 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND SUBSTRATE.
[5]"Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants."
Mininno M., Brugiere S., Pautre V., Gilgen A., Ma S., Ferro M., Tardif M., Alban C., Ravanel S.
J. Biol. Chem. 287:21034-21044(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L34291 mRNA. Translation: AAA69903.1.
PIRS53005.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MLVX-ray2.60A/B/C46-482[»]
1OZVX-ray2.65A/B/C46-482[»]
1P0YX-ray2.55A/B/C46-482[»]
2H21X-ray2.45A/B/C49-482[»]
2H23X-ray2.45A/B/C49-482[»]
2H2EX-ray2.60A/B/C49-482[»]
2H2JX-ray2.45A/B/C49-482[»]
ProteinModelPortalQ43088.
SMRQ43088. Positions 48-485.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48722N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.1420.10. 1 hit.
InterProIPR015353. Rubisco_LSMT_subst-bd.
IPR011192. Rubisco_MeTrfase.
IPR001214. SET_dom.
[Graphical view]
PfamPF09273. Rubis-subs-bind. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFPIRSF009328. RMT_SET. 1 hit.
SMARTSM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF81822. Rubisco_LSMT_subst-bd. 1 hit.
PROSITEPS50280. SET. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ43088.

Entry information

Entry nameRBCMT_PEA
AccessionPrimary (citable) accession number: Q43088
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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