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P34915

- RBL_PHYPA

UniProt

P34915 - RBL_PHYPA

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Physcomitrella patens subsp. patens (Moss)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (07 Nov 2003)
      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
    Encoded oniPlastid; Chloroplast
    OrganismiPhyscomitrella patens subsp. patens (Moss)
    Taxonomic identifieri3218 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella
    ProteomesiUP000006727: 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_0000031347
    Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_0000031348Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylprolineUniRule annotation
    Modified residuei14 – 141N6,N6,N6-trimethyllysineUniRule annotation
    Modified residuei201 – 2011N6-carboxylysineUniRule annotation
    Disulfide bondi247 – 247Interchain; in linked formUniRule annotation

    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.UniRule annotation

    Keywords - PTMi

    Acetylation, Disulfide bond, Methylation

    Proteomic databases

    PRIDEiP34915.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP34915.
    SMRiP34915. Positions 18-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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.

    P34915-1 [UniParc]FASTAAdd to Basket

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    MSPRPEIKAG VGFKAGVKDY RLTYYTPDYQ TKDTDILAAF RMTPQPGVPA    50
    EECGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYAIEPV AGEENQYIAY 100
    VAYPLDLFEE GSVTNLFTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFQG 150
    PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
    KDDENVNSQP FMRWRDRFLF CAEAIYKSQG ETGEIKGHYL NATAGTCEEM 250
    IKRAQFAREL GMPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 300
    LDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERQ VTLGFVDLLR 350
    DDYIEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL 400
    QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREAAK 450
    WSPELAAACE VWKEIKFEFD TVDTL 475
    Length:475
    Mass (Da):52,705
    Last modified:November 7, 2003 - v2
    Checksum:i30A91B8A714507AF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91A → T in CAA52269. 1 PublicationCurated
    Sequence conflicti30 – 301Q → H in CAA52269. 1 PublicationCurated
    Sequence conflicti50 – 501A → L in CAA52269. 1 PublicationCurated
    Sequence conflicti190 – 1901Y → N in CAA52269. 1 PublicationCurated
    Sequence conflicti251 – 2511I → L in CAA52269. 1 PublicationCurated
    Sequence conflicti255 – 2562QF → PC in CAA52269. 1 PublicationCurated
    Sequence conflicti301 – 3011L → V in CAA52269. 1 PublicationCurated
    Sequence conflicti339 – 3391R → L in CAA52269. 1 PublicationCurated
    Sequence conflicti372 – 3743PGV → QVF in CAA52269. 1 PublicationCurated
    Sequence conflicti385 – 3851W → G in CAA52269. 1 PublicationCurated
    Sequence conflicti414 – 4141A → T in CAA52269. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74156 Genomic DNA. Translation: CAA52269.1.
    AB066207 Genomic DNA. Translation: BAB62086.1.
    AP005672 Genomic DNA. Translation: BAC85044.1.
    PIRiS34663.
    RefSeqiNP_904194.1. NC_005087.1.

    Genome annotation databases

    GeneIDi2546763.
    KEGGippp:PhpapaCp031.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74156 Genomic DNA. Translation: CAA52269.1 .
    AB066207 Genomic DNA. Translation: BAB62086.1 .
    AP005672 Genomic DNA. Translation: BAC85044.1 .
    PIRi S34663.
    RefSeqi NP_904194.1. NC_005087.1.

    3D structure databases

    ProteinModelPortali P34915.
    SMRi P34915. Positions 18-473.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P34915.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2546763.
    KEGGi ppp:PhpapaCp031.

    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. "An open reading frame (ycf11) is evolutionary conserved from Cyanobacteria to the plastid DNAs of Archegoniates and Gymnosperms is modified in the plastid DNAs of Dicots and is not plastome encoded in Monocots."
      Kruse S., Martin W., Wehe M., Reski R.
      J. Plant Physiol. 146:258-262(1995)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Physcomitrella patens chloroplast genes."
      Sugita M., Sugiura C.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Protonema.
    3. "Complete chloroplast DNA sequence of the moss Physcomitrella patens: evidence for the loss and relocation of rpoA from the chloroplast to the nucleus."
      Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.
      Nucleic Acids Res. 31:5324-5331(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Gransden 2004.
    4. "Cytokinin affects nuclear- and plastome-encoded energy-converting plastid enzymes."
      Kasten B., Buck F., Nuske J., Reski R.
      Planta 201:261-272(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 184-195.
      Tissue: Protonema.

    Entry informationi

    Entry nameiRBL_PHYPA
    AccessioniPrimary (citable) accession number: P34915
    Secondary accession number(s): Q95FY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: November 7, 2003
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3