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Q0P3J3

- RBL_OSTTA

UniProt

Q0P3J3 - RBL_OSTTA

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Ostreococcus tauri
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (19 Sep 2006)
      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.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei123 – 1231Substrate; in homodimeric partnerUniRule annotation
    Binding sitei173 – 1731SubstrateUniRule annotation
    Active sitei175 – 1751Proton acceptorUniRule annotation
    Binding sitei177 – 1771SubstrateUniRule annotation
    Metal bindingi201 – 2011Magnesium; via carbamate groupUniRule annotation
    Metal bindingi203 – 2031MagnesiumUniRule annotation
    Metal bindingi204 – 2041MagnesiumUniRule annotation
    Active sitei294 – 2941Proton acceptorUniRule annotation
    Binding sitei295 – 2951SubstrateUniRule annotation
    Binding sitei327 – 3271SubstrateUniRule annotation
    Sitei334 – 3341Transition state stabilizerUniRule annotation
    Binding sitei379 – 3791SubstrateUniRule annotation

    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 chainUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunitUniRule annotation
    Gene namesi
    Name:rbcLUniRule annotation
    Ordered Locus Names:OtCpg00590
    Encoded oniPlastid; Chloroplast
    OrganismiOstreococcus tauri
    Taxonomic identifieri70448 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeChlorophytaMamiellophyceaeMamiellalesOstreococcus
    ProteomesiUP000009170: Chloroplast

    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 – 22UniRule annotationPRO_0000251427
    Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_0000251428Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylprolineUniRule annotation
    Modified residuei201 – 2011N6-carboxylysineUniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ0P3J3.

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

    Protein-protein interaction databases

    STRINGi70448.Q0P3J3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0P3J3.
    SMRiQ0P3J3. Positions 12-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    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.

    Q0P3J3-1 [UniParc]FASTAAdd to Basket

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    MAPQTETKTG TGFQAGVKDY RLTYYTPDYQ VKETDILAAF RMTPQPGVPA    50
    EECGAAVAAE SSTGTWTTVW TDGLTQLDRY KGRCYDLEPV PGEDNQFIAY 100
    VAYPLDLFEE GSVTNLFTSI VGNVFGFKAL RALRLEDLRI PVAYCKTFQG 150
    APHGIQTERD KLNKYGRGLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
    KDDENVNSQP FMRWRDRFLF VAEAIYKSQA ETGEIKGHYL NATAGNVDQM 250
    LKRAQVAKEL GMPIIMHDYL TAGFTANTTL ATYCREEGLL LHIHRAMHAV 300
    IDRQRNHGIH FRVLAKALRL SGGDHLHSGT VVGKLEGERN VTLGFVDLMR 350
    DAYVEKDRDR GIYFSQDWAS LPGVMPVASG GIHVWHMPAL VEIFGDDACL 400
    QFGGGTLGHP WGNAPGASAN RVALEACTQA RNEGRDLARE GGDVIRAACK 450
    WSPELAAACE VWKEIKFEFD TVDTL 475
    Length:475
    Mass (Da):52,520
    Last modified:September 19, 2006 - v1
    Checksum:i90EFD83EA2992B11
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR954199 Genomic DNA. Translation: CAL36384.1.
    RefSeqiYP_717262.1. NC_008289.1.

    Genome annotation databases

    GeneIDi4238788.
    KEGGiota:OstapCp59.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR954199 Genomic DNA. Translation: CAL36384.1 .
    RefSeqi YP_717262.1. NC_008289.1.

    3D structure databases

    ProteinModelPortali Q0P3J3.
    SMRi Q0P3J3. Positions 12-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 70448.Q0P3J3.

    Proteomic databases

    PRIDEi Q0P3J3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4238788.
    KEGGi ota:OstapCp59.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    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. "The complete chloroplast and mitochondrial DNA sequence of Ostreococcus tauri: organelle genomes of the smallest eukaryote are examples of compaction."
      Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H., Van de Peer Y.
      Mol. Biol. Evol. 24:956-968(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: OTTH0595.

    Entry informationi

    Entry nameiRBL_OSTTA
    AccessioniPrimary (citable) accession number: Q0P3J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: September 19, 2006
    Last modified: October 1, 2014
    This is version 46 of the entry and version 1 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".UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3