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Q33015

- RBL_PTEVI

UniProt

Q33015 - RBL_PTEVI

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Pteris vittata (Chinese ladder brake)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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 sitei113 – 1131Substrate; in homodimeric partnerUniRule annotation
    Binding sitei163 – 1631SubstrateUniRule annotation
    Active sitei165 – 1651Proton acceptorUniRule annotation
    Binding sitei167 – 1671SubstrateUniRule annotation
    Metal bindingi191 – 1911Magnesium; via carbamate groupUniRule annotation
    Metal bindingi193 – 1931MagnesiumUniRule annotation
    Metal bindingi194 – 1941MagnesiumUniRule annotation
    Active sitei284 – 2841Proton acceptorUniRule annotation
    Binding sitei285 – 2851SubstrateUniRule annotation
    Binding sitei317 – 3171SubstrateUniRule annotation
    Sitei324 – 3241Transition state stabilizerUniRule annotation
    Binding sitei369 – 3691SubstrateUniRule annotation

    GO - Molecular functioni

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

    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
    OrganismiPteris vittata (Chinese ladder brake)
    Taxonomic identifieri13821 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaMoniliformopsesPolypodiidaePolypodialesPteridaceaePteris

    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
    Chaini‹1 – ›440›440Ribulose bisphosphate carboxylase large chainPRO_0000062577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41N6,N6,N6-trimethyllysineUniRule annotation
    Modified residuei191 – 1911N6-carboxylysineUniRule annotation
    Disulfide bondi237 – 237Interchain; 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

    Disulfide bond, Methylation

    Proteomic databases

    PRIDEiQ33015.

    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

    ProteinModelPortaliQ33015.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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: Fragment.

    Q33015-1 [UniParc]FASTAAdd to Basket

    « Hide

    VGFKAGVKDY RLTYYTPEYK TKDTDILAAF RMTPQPGVPA EEAGAAVAAE    50
    SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV AGEENQYIAY VAYPLDLFEE 100
    GSVTNMLTSI VGNVFGXKAX RALRLEDLRI LPAYSKTFIG PPHGIQVERD 150
    KLNKYGRPLL GCTIKPKLGL CAKNYGRAVY ECLRGGLDFT KDDENVNSQP 200
    SMRWRDRFLF VAEALFKAQA ETGEVKGHYL NATAGTCEEM IKRATFAREL 250
    GAPIVMHDYL TGGFTANTSL AFYCRDNGLL LHIHRAMHAV IDRQRNHGMH 300
    LRVLAKALRM SGGDHIHAGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR 350
    GIYFTQDWVS MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP 400
    WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK 440
    Length:440
    Mass (Da):48,575
    Last modified:November 1, 1997 - v1
    Checksum:i904A064E8BB40578
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei440 – 4401

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05941 Genomic DNA. Translation: AAC48966.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05941 Genomic DNA. Translation: AAC48966.1 .

    3D structure databases

    ProteinModelPortali Q33015.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q33015.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Phylogenetic relationships of dennstaedtioid ferns: evidence from rbcL sequences."
      Wolf P.G., Soltis P.S., Soltis D.E.
      Mol. Phylogenet. Evol. 3:383-392(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leaf.

    Entry informationi

    Entry nameiRBL_PTEVI
    AccessioniPrimary (citable) accession number: Q33015
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 73 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3