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P92397

- RBL_LUPAL

UniProt

P92397 - RBL_LUPAL

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Lupinus albus (White lupin) (Lupinus termis)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 May 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 sitei114 – 1141Substrate; in homodimeric partnerUniRule annotation
    Binding sitei164 – 1641SubstrateUniRule annotation
    Active sitei166 – 1661Proton acceptorUniRule annotation
    Binding sitei168 – 1681SubstrateUniRule annotation
    Metal bindingi192 – 1921Magnesium; via carbamate groupUniRule annotation
    Metal bindingi194 – 1941MagnesiumUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Active sitei285 – 2851Proton acceptorUniRule annotation
    Binding sitei286 – 2861SubstrateUniRule annotation
    Binding sitei318 – 3181SubstrateUniRule annotation
    Sitei325 – 3251Transition state stabilizerUniRule annotation
    Binding sitei370 – 3701SubstrateUniRule 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
    OrganismiLupinus albus (White lupin) (Lupinus termis)
    Taxonomic identifieri3870 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeGenisteaeLupinus

    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 – ›455›455Ribulose bisphosphate carboxylase large chainPRO_0000062508Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6,N6,N6-trimethyllysineUniRule annotation
    Modified residuei192 – 1921N6-carboxylysineUniRule annotation
    Disulfide bondi238 – 238Interchain; 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

    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

    ProteinModelPortaliP92397.
    SMRiP92397. Positions 9-455.
    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.

    P92397-1 [UniParc]FASTAAdd to Basket

    « Hide

    SVGFKAGVKD YKLTYYTPDY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA    50
    ESSTGTWTTV WTDGLTSLDR YKGRCYHIEP VAGEENQFIA YVAYPLDLFE 100
    EGSVTNMFTS IVGNVFGFKA LRALRLEDLR IPNAYVKTFQ GPPHGIQVER 150
    DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF TKDDENVNSQ 200
    PFMRWRDRFL FCAEALYKAQ AETGEIKGHY LNATAGTCEE MIKRAVFARE 250
    LGVPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM 300
    HFRVLAKALR LSGGDHIHSG TVVGKLEGER EITLGFVDLL RDDFVEKDRS 350
    RGIYFTQDWV SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH 400
    PWGNAPGAVA NRVALEACVQ ARNEGRDLAS EGNQIIREAS KWSPELAAAC 450
    EVWKE 455
    Length:455
    Mass (Da):50,315
    Last modified:May 1, 1997 - v1
    Checksum:iFC9AD8CF670CE339
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei455 – 4551

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z70068 Genomic DNA. Translation: CAA93927.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z70068 Genomic DNA. Translation: CAA93927.1 .

    3D structure databases

    ProteinModelPortali P92397.
    SMRi P92397. Positions 9-455.
    ModBasei Search...
    MobiDBi Search...

    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. "Molecular phylogeny of the Papilionoideae (family Leguminosae): rbcL sequences versus chemical taxonomy."
      Kaess E., Wink M.
      Bot. Acta 108:149-162(1995)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leaf.

    Entry informationi

    Entry nameiRBL_LUPAL
    AccessioniPrimary (citable) accession number: P92397
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 72 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