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Q43088

- RBCMT_PEA

UniProt

Q43088 - RBCMT_PEA

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
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

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    MATIFSGGSV SPFLFHTNKG TSFTPKAPIL HLKRSFSAKS VASVGTEPSL    50
    SPAVQTFWKW LQEEGVITAK TPVKASVVTE GLGLVALKDI SRNDVILQVP 100
    KRLWINPDAV AASEIGRVCS ELKPWLSVIL FLIRERSRED SVWKHYFGIL 150
    PQETDSTIYW SEEELQELQG SQLLKTTVSV KEYVKNECLK LEQEIILPNK 200
    RLFPDPVTLD DFFWAFGILR SRAFSRLRNE NLVVVPMADL INHSAGVTTE 250
    DHAYEVKGAA GLFSWDYLFS LKSPLSVKAG EQVYIQYDLN KSNAELALDY 300
    GFIEPNENRH AYTLTLEISE SDPFFDDKLD VAESNGFAQT AYFDIFYNRT 350
    LPPGLLPYLR LVALGGTDAF LLESLFRDTI WGHLELSVSR DNEELLCKAV 400
    REACKSALAG YHTTIEQDRE LKEGNLDSRL AIAVGIREGE KMVLQQIDGI 450
    FEQKELELDQ LEYYQERRLK DLGLCGENGD ILGDLGKFF 489
    Length:489
    Mass (Da):55,110
    Last modified:November 1, 1996 - v1
    Checksum:i72C53E37EE08AFC5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34291 mRNA. Translation: AAA69903.1.
    PIRiS53005.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L34291 mRNA. Translation: AAA69903.1 .
    PIRi S53005.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 86 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