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P27064

- RBL_CUCSA

UniProt

P27064 - RBL_CUCSA

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Cucumis sativus (Cucumber)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 5 (11 Sep 2007)
      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
    Ordered Locus Names:CsCp048
    Encoded oniPlastid; Chloroplast
    OrganismiCucumis sativus (Cucumber)
    Taxonomic identifieri3659 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

    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_0000031195
    Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_0000031196Add
    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

    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

    3D structure databases

    ProteinModelPortaliP27064.
    SMRiP27064. Positions 18-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK01601.

    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.

    P27064-1 [UniParc]FASTAAdd to Basket

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    MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP    50
    EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYGIEPV AGEENQYIAY 100
    VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PTAYIKTFQG 150
    PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
    KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL NATAGTCEEM 250
    MKRAIFAREL GAPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 300
    IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR 350
    DDFVEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL 400
    QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK 450
    WSPELAAACE VWKEIKFEFE AMDTL 475
    Length:475
    Mass (Da):52,642
    Last modified:September 11, 2007 - v5
    Checksum:iF03D68FF32EEB6B4
    GO

    Sequence cautioni

    The sequence AAZ94659.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti117 – 1171F → V in AAA84187. 1 PublicationCurated
    Sequence conflicti117 – 1171F → V in AAL35646. 1 PublicationCurated
    Sequence conflicti237 – 2393GHY → DI in CAJ00766. (PubMed:17607527)Curated
    Sequence conflicti456 – 4627AAACEVW → VCVTWRKYG in CAJ00766. (PubMed:17607527)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ119058 Genomic DNA. Translation: AAZ94659.1. Different initiation.
    AJ970307 Genomic DNA. Translation: CAJ00766.1.
    DQ865975 Genomic DNA. Translation: ABI97425.1.
    DQ865976 Genomic DNA. Translation: ABI98753.1.
    L21937 Genomic DNA. Translation: AAA84187.1.
    AF206755 Genomic DNA. Translation: AAL35646.1.
    RefSeqiYP_247607.1. NC_007144.1.

    Genome annotation databases

    GeneIDi3429289.
    KEGGicsv:3429289.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ119058 Genomic DNA. Translation: AAZ94659.1 . Different initiation.
    AJ970307 Genomic DNA. Translation: CAJ00766.1 .
    DQ865975 Genomic DNA. Translation: ABI97425.1 .
    DQ865976 Genomic DNA. Translation: ABI98753.1 .
    L21937 Genomic DNA. Translation: AAA84187.1 .
    AF206755 Genomic DNA. Translation: AAL35646.1 .
    RefSeqi YP_247607.1. NC_007144.1.

    3D structure databases

    ProteinModelPortali P27064.
    SMRi P27064. Positions 18-473.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3429289.
    KEGGi csv:3429289.

    Phylogenomic databases

    KOi K01601.

    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. "Complete sequence and organization of the cucumber (Cucumis sativus L. cv. Baekmibaekdadagi) chloroplast genome."
      Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J., Choi D.-W., Liu J.R., Cho K.Y.
      Plant Cell Rep. 25:334-340(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Baekmibaekdadagi.
    2. "The complete structure of the cucumber (Cucumis sativus L.) chloroplast genome: its composition and comparative analysis."
      Plader W.W., Yukawa Y., Sugiura M., Malepszy S.
      Cell. Mol. Biol. Lett. 12:584-594(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Borszczagowski.
    3. "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies differences between chilling-tolerant and -susceptible cucumber lines."
      Chung S.-M., Gordon V.S., Staub J.E.
      Genome 50:215-225(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Chipper and cv. Gy14.
    4. "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.
    5. "Phylogenetic affinites of Datiscaceae based on an analysis of nucleotide sequences from the plastid rbcL gene."
      Swensen S.M., Mullin B.C., Chase M.W.
      Syst. Bot. 19:157-168(1994)
      [AGRICOLA] [Europe PMC]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-473.
    6. "Angiosperm phylogeny inferred from multiple genes as a tool for comparative biology."
      Soltis P.S., Soltis D.E., Chase M.W.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-473.

    Entry informationi

    Entry nameiRBL_CUCSA
    AccessioniPrimary (citable) accession number: P27064
    Secondary accession number(s): A5J1U2
    , Q2QD81, Q32077, Q4VZI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 89 of the entry and version 5 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3