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Protein

Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic

Gene

RBCMT

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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.
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.

Kineticsi

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

  1. KM=12.9 µM for fructose-bisphosphate aldolase 22 Publications
  2. KM=14.0 µM for fructose-bisphosphate aldolase 32 Publications
  3. KM=32.0 µM for gamma-tocopherol methyltransferase2 Publications
  4. KM=4.5 µM for rubisco2 Publications
  5. KM=6 µM for S-adenosyl-L-methionine2 Publications
  1. Vmax=19.5 nmol/min/mg enzyme with fructose-bisphosphate aldolase 2 as substrate2 Publications
  2. Vmax=9.0 nmol/min/mg enzyme with fructose-bisphosphate aldolase 3 as substrate2 Publications
  3. Vmax=1.7 nmol/min/mg enzyme with gamma-tocopherol methyltransferase as substrate2 Publications
  4. Vmax=44.6 nmol/min/mg enzyme with rubisco as substrate2 Publications
  5. Vmax=56 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei222S-adenosyl-L-methioninePROSITE-ProRule annotation3 Publications1
Binding sitei222Substrate; via carbonyl oxygen2 Publications1
Binding sitei226Substrate2 Publications1
Binding sitei239Substrate; via carbonyl oxygen2 Publications1
Binding sitei254Substrate2 Publications1
Binding sitei287Substrate2 Publications1
Binding sitei300Substrate2 Publications1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.127. 4872.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RBCMT
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi281E → Q: No effect on substrate affinity, but reduced catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 37ChloroplastSequence analysisAdd BLAST37
ChainiPRO_000002219938 – 489Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplasticAdd BLAST452

Expressioni

Tissue specificityi

Highly expressed in leaf.

Interactioni

Subunit structurei

Homotrimer.3 Publications

Protein-protein interaction databases

DIPiDIP-48722N.

Structurei

Secondary structure

1489
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi52 – 63Combined sources12
Beta strandi66 – 70Combined sources5
Beta strandi72 – 78Combined sources7
Beta strandi81 – 88Combined sources8
Beta strandi94 – 100Combined sources7
Helixi101 – 103Combined sources3
Helixi107 – 110Combined sources4
Helixi116 – 119Combined sources4
Beta strandi120 – 122Combined sources3
Helixi124 – 137Combined sources14
Helixi144 – 147Combined sources4
Turni157 – 159Combined sources3
Helixi162 – 166Combined sources5
Turni167 – 170Combined sources4
Helixi172 – 194Combined sources23
Turni198 – 202Combined sources5
Helixi209 – 222Combined sources14
Beta strandi226 – 229Combined sources4
Beta strandi231 – 233Combined sources3
Helixi238 – 240Combined sources3
Beta strandi253 – 255Combined sources3
Helixi258 – 260Combined sources3
Helixi264 – 266Combined sources3
Beta strandi268 – 275Combined sources8
Beta strandi281 – 285Combined sources5
Helixi293 – 299Combined sources7
Helixi307 – 309Combined sources3
Beta strandi311 – 317Combined sources7
Helixi325 – 333Combined sources9
Turni334 – 336Combined sources3
Beta strandi339 – 346Combined sources8
Helixi355 – 363Combined sources9
Helixi366 – 372Combined sources7
Helixi374 – 376Combined sources3
Turni377 – 379Combined sources3
Helixi380 – 386Combined sources7
Helixi390 – 408Combined sources19
Beta strandi411 – 413Combined sources3
Helixi415 – 422Combined sources8
Helixi428 – 456Combined sources29
Turni457 – 460Combined sources4
Helixi464 – 469Combined sources6
Beta strandi474 – 476Combined sources3
Helixi479 – 482Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ43088.
SMRiQ43088.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ43088.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 288SETPROSITE-ProRule annotationAdd BLAST225

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni80 – 82S-adenosyl-L-methionine binding3
Regioni242 – 243S-adenosyl-L-methionine binding2

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Plant protein-lysine LSMT methyltransferase family.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.90.1420.10. 1 hit.
InterProiIPR011192. Rubisco_LSMT_MeTrfase_plant.
IPR015353. Rubisco_LSMT_subst-bd.
IPR001214. SET_dom.
[Graphical view]
PfamiPF09273. Rubis-subs-bind. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009328. RMT_SET. 1 hit.
SMARTiSM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF81822. SSF81822. 1 hit.
PROSITEiPS51583. SAM_MT127. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q43088-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATIFSGGSV SPFLFHTNKG TSFTPKAPIL HLKRSFSAKS VASVGTEPSL
60 70 80 90 100
SPAVQTFWKW LQEEGVITAK TPVKASVVTE GLGLVALKDI SRNDVILQVP
110 120 130 140 150
KRLWINPDAV AASEIGRVCS ELKPWLSVIL FLIRERSRED SVWKHYFGIL
160 170 180 190 200
PQETDSTIYW SEEELQELQG SQLLKTTVSV KEYVKNECLK LEQEIILPNK
210 220 230 240 250
RLFPDPVTLD DFFWAFGILR SRAFSRLRNE NLVVVPMADL INHSAGVTTE
260 270 280 290 300
DHAYEVKGAA GLFSWDYLFS LKSPLSVKAG EQVYIQYDLN KSNAELALDY
310 320 330 340 350
GFIEPNENRH AYTLTLEISE SDPFFDDKLD VAESNGFAQT AYFDIFYNRT
360 370 380 390 400
LPPGLLPYLR LVALGGTDAF LLESLFRDTI WGHLELSVSR DNEELLCKAV
410 420 430 440 450
REACKSALAG YHTTIEQDRE LKEGNLDSRL AIAVGIREGE KMVLQQIDGI
460 470 480
FEQKELELDQ LEYYQERRLK DLGLCGENGD ILGDLGKFF
Length:489
Mass (Da):55,110
Last modified:November 1, 1996 - v1
Checksum:i72C53E37EE08AFC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34291 mRNA. Translation: AAA69903.1.
PIRiS53005.

Genome annotation databases

KEGGiag:AAA69903.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34291 mRNA. Translation: AAA69903.1.
PIRiS53005.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ43088.
SMRiQ43088.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48722N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA69903.

Enzyme and pathway databases

BRENDAi2.1.1.127. 4872.

Miscellaneous databases

EvolutionaryTraceiQ43088.

Family and domain databases

Gene3Di3.90.1420.10. 1 hit.
InterProiIPR011192. Rubisco_LSMT_MeTrfase_plant.
IPR015353. Rubisco_LSMT_subst-bd.
IPR001214. SET_dom.
[Graphical view]
PfamiPF09273. Rubis-subs-bind. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF009328. RMT_SET. 1 hit.
SMARTiSM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF81822. SSF81822. 1 hit.
PROSITEiPS51583. SAM_MT127. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRBCMT_PEA
AccessioniPrimary (citable) accession number: Q43088
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.