Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q43088

- RBCMT_PEA

UniProt

Q43088 - RBCMT_PEA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene

RBCMT

Organism
Pisum sativum (Garden pea)
Status
Reviewed - 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

Vmax=19.5 nmol/min/mg enzyme with fructose-bisphosphate aldolase 2 as substrate2 Publications

Vmax=9.0 nmol/min/mg enzyme with fructose-bisphosphate aldolase 3 as substrate2 Publications

Vmax=1.7 nmol/min/mg enzyme with gamma-tocopherol methyltransferase as substrate2 Publications

Vmax=44.6 nmol/min/mg enzyme with rubisco as substrate2 Publications

Vmax=56 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei222 – 2221S-adenosyl-L-methionine3 PublicationsPROSITE-ProRule annotation
Binding sitei222 – 2221Substrate; via carbonyl oxygen2 Publications
Binding sitei226 – 2261Substrate2 Publications
Binding sitei239 – 2391Substrate; via carbonyl oxygen2 Publications
Binding sitei254 – 2541Substrate2 Publications
Binding sitei287 – 2871Substrate2 Publications
Binding sitei300 – 3001Substrate2 Publications

GO - Molecular functioni

  1. [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

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

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi281 – 2811E → Q: No effect on substrate affinity, but reduced catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737ChloroplastSequence AnalysisAdd
BLAST
Chaini38 – 489452Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplasticPRO_0000022199Add
BLAST

Expressioni

Tissue specificityi

Highly expressed in leaf.

Interactioni

Subunit structurei

Homotrimer.3 Publications

Protein-protein interaction databases

DIPiDIP-48722N.

Structurei

Secondary structure

1
489
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi52 – 6312Combined sources
Beta strandi66 – 705Combined sources
Beta strandi72 – 787Combined sources
Beta strandi81 – 888Combined sources
Beta strandi94 – 1007Combined sources
Helixi101 – 1033Combined sources
Helixi107 – 1104Combined sources
Helixi116 – 1194Combined sources
Beta strandi120 – 1223Combined sources
Helixi124 – 13714Combined sources
Helixi144 – 1474Combined sources
Turni157 – 1593Combined sources
Helixi162 – 1665Combined sources
Turni167 – 1704Combined sources
Helixi172 – 19423Combined sources
Turni198 – 2025Combined sources
Helixi209 – 22214Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi231 – 2333Combined sources
Helixi238 – 2403Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi268 – 2758Combined sources
Beta strandi281 – 2855Combined sources
Helixi293 – 2997Combined sources
Helixi307 – 3093Combined sources
Beta strandi311 – 3177Combined sources
Helixi325 – 3339Combined sources
Turni334 – 3363Combined sources
Beta strandi339 – 3468Combined sources
Helixi355 – 3639Combined sources
Helixi366 – 3727Combined sources
Helixi374 – 3763Combined sources
Turni377 – 3793Combined sources
Helixi380 – 3867Combined sources
Helixi390 – 40819Combined sources
Beta strandi411 – 4133Combined sources
Helixi415 – 4228Combined sources
Helixi428 – 45629Combined sources
Turni457 – 4604Combined sources
Helixi464 – 4696Combined sources
Beta strandi474 – 4763Combined sources
Helixi479 – 4824Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 48-485.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ43088.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 288225SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 823S-adenosyl-L-methionine binding
Regioni242 – 2432S-adenosyl-L-methionine binding

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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34291 mRNA. Translation: AAA69903.1 .
PIRi S53005.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MLV X-ray 2.60 A/B/C 46-482 [» ]
1OZV X-ray 2.65 A/B/C 46-482 [» ]
1P0Y X-ray 2.55 A/B/C 46-482 [» ]
2H21 X-ray 2.45 A/B/C 49-482 [» ]
2H23 X-ray 2.45 A/B/C 49-482 [» ]
2H2E X-ray 2.60 A/B/C 49-482 [» ]
2H2J X-ray 2.45 A/B/C 49-482 [» ]
ProteinModelPortali Q43088.
SMRi Q43088. Positions 48-485.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48722N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q43088.

Family and domain databases

Gene3Di 3.90.1420.10. 1 hit.
InterProi IPR011192. Rubisco_LSMT_MeTrfase_plant.
IPR015353. Rubisco_LSMT_subst-bd.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF09273. Rubis-subs-bind. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
PIRSFi PIRSF009328. RMT_SET. 1 hit.
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF81822. SSF81822. 1 hit.
PROSITEi PS51583. SAM_MT127. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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 26, 2014
This is version 88 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

External Data

Dasty 3