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P04717

- RBL_PEA

UniProt

P04717 - RBL_PEA

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

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 98 (01 Oct 2014)
      Sequence version 3 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.

    Catalytic activityi

    2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei123 – 1231Substrate; in homodimeric partnerBy similarity
    Binding sitei173 – 1731SubstrateBy similarity
    Active sitei175 – 1751Proton acceptorBy similarity
    Binding sitei177 – 1771SubstrateBy similarity
    Metal bindingi201 – 2011Magnesium; via carbamate groupBy similarity
    Metal bindingi203 – 2031MagnesiumBy similarity
    Metal bindingi204 – 2041MagnesiumBy similarity
    Active sitei294 – 2941Proton acceptorBy similarity
    Binding sitei295 – 2951SubstrateBy similarity
    Binding sitei327 – 3271SubstrateBy similarity
    Sitei334 – 3341Transition state stabilizerBy similarity
    Binding sitei379 – 3791SubstrateBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB-HAMAP
    2. monooxygenase activity Source: UniProtKB-KW
    3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. photorespiration Source: UniProtKB-KW
    2. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
    Short name:
    RuBisCO large subunit
    Gene namesi
    Name:rbcL
    Encoded oniPlastid; Chloroplast
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 221 PublicationPRO_0000031333
    Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_0000031334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylproline1 Publication
    Modified residuei14 – 141N6,N6,N6-trimethyllysine1 Publication
    Modified residuei201 – 2011N6-carboxylysineBy similarity
    Disulfide bondi247 – 247Interchain; in linked formBy similarity

    Post-translational modificationi

    The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Methylation

    Proteomic databases

    PRIDEiP04717.

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.By similarity

    Structurei

    Secondary structure

    1
    475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 244
    Beta strandi36 – 449
    Helixi50 – 6011
    Turni61 – 633
    Beta strandi66 – 683
    Helixi70 – 745
    Helixi77 – 804
    Beta strandi83 – 897
    Beta strandi91 – 944
    Beta strandi97 – 1037
    Helixi105 – 1073
    Helixi113 – 1219
    Helixi124 – 1263
    Beta strandi130 – 13910
    Helixi142 – 1454
    Beta strandi151 – 1533
    Helixi155 – 1628
    Beta strandi169 – 1713
    Beta strandi175 – 1784
    Helixi182 – 19413
    Beta strandi198 – 2014
    Beta strandi207 – 2093
    Helixi214 – 23219
    Beta strandi237 – 2415
    Helixi247 – 26014
    Beta strandi263 – 2686
    Helixi269 – 2724
    Helixi274 – 28714
    Beta strandi290 – 2945
    Helixi298 – 3025
    Beta strandi305 – 3095
    Helixi311 – 32111
    Beta strandi324 – 3274
    Beta strandi331 – 3355
    Helixi339 – 35012
    Beta strandi352 – 3543
    Helixi358 – 3603
    Beta strandi375 – 3817
    Helixi384 – 3863
    Helixi387 – 3948
    Beta strandi399 – 4013
    Helixi404 – 4074
    Helixi413 – 43220
    Helixi437 – 44812
    Turni449 – 4513
    Helixi453 – 46210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HHHX-ray2.20A/B/C/D1-475[»]
    4MKVX-ray2.15A/B/C/D12-469[»]
    ProteinModelPortaliP04717.
    SMRiP04717. Positions 9-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01338. RuBisCO_L_type1.
    InterProiIPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    IPR000685. RuBisCO_lsu_C.
    IPR017443. RuBisCO_lsu_fd_N.
    IPR017444. RuBisCO_lsu_N.
    [Graphical view]
    PfamiPF00016. RuBisCO_large. 1 hit.
    PF02788. RuBisCO_large_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51649. SSF51649. 1 hit.
    SSF54966. SSF54966. 1 hit.
    PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P04717-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPQTETKAK VGFKAGVKDY KLTYYTPDYQ TKDTDILAAF RVTPQPGVPP    50
    EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYEIEPV PGEDNQFIAY 100
    VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PYAYVKTFQG 150
    PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
    KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL NATAGTCEEM 250
    LKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV 300
    IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERE ITLGFVDLLR 350
    DDYIKKDRSR GIYFTQDWVS LPGVIPVASG GIHVWHMPAL TEIFGDDSVL 400
    QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNAIIREACK 450
    WSPELAAACE VWKEIKFEFP AMDTL 475
    Length:475
    Mass (Da):52,763
    Last modified:December 1, 1992 - v3
    Checksum:i1F673855DD921DF9
    GO

    Sequence cautioni

    The sequence CAA27483.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03853 Genomic DNA. Translation: CAA27483.1. Different initiation.
    PIRiA24471. RKPMLC.
    RefSeqiYP_003587524.1. NC_014057.1.

    Genome annotation databases

    GeneIDi9073048.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03853 Genomic DNA. Translation: CAA27483.1 . Different initiation.
    PIRi A24471. RKPMLC.
    RefSeqi YP_003587524.1. NC_014057.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HHH X-ray 2.20 A/B/C/D 1-475 [» ]
    4MKV X-ray 2.15 A/B/C/D 12-469 [» ]
    ProteinModelPortali P04717.
    SMRi P04717. Positions 9-475.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P04717.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 9073048.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01338. RuBisCO_L_type1.
    InterProi IPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    IPR000685. RuBisCO_lsu_C.
    IPR017443. RuBisCO_lsu_fd_N.
    IPR017444. RuBisCO_lsu_N.
    [Graphical view ]
    Pfami PF00016. RuBisCO_large. 1 hit.
    PF02788. RuBisCO_large_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51649. SSF51649. 1 hit.
    SSF54966. SSF54966. 1 hit.
    PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from pea chloroplasts."
      Zurawski G., Whitfeld P.R., Bottomley W.
      Nucleic Acids Res. 14:3975-3976(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species."
      Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.
      Plant Physiol. 98:1170-1174(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14, ACETYLATION AT PRO-3.

    Entry informationi

    Entry nameiRBL_PEA
    AccessioniPrimary (citable) accession number: P04717
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 98 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity.By similarity

    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