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P48699

- RBL_DENCL

UniProt

P48699 - RBL_DENCL

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Dendrophthora clavata (Columbian mistletoe)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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 sitei122 – 1221Substrate; in homodimeric partnerUniRule annotation
    Binding sitei172 – 1721SubstrateUniRule annotation
    Active sitei174 – 1741Proton acceptorUniRule annotation
    Binding sitei176 – 1761SubstrateUniRule annotation
    Metal bindingi200 – 2001Magnesium; via carbamate groupUniRule annotation
    Metal bindingi202 – 2021MagnesiumUniRule annotation
    Metal bindingi203 – 2031MagnesiumUniRule annotation
    Active sitei293 – 2931Proton acceptorUniRule annotation
    Binding sitei294 – 2941SubstrateUniRule annotation
    Binding sitei326 – 3261SubstrateUniRule annotation
    Sitei333 – 3331Transition state stabilizerUniRule annotation
    Binding sitei378 – 3781SubstrateUniRule 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
    OrganismiDendrophthora clavata (Columbian mistletoe)
    Taxonomic identifieri3965 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeDendrophthora

    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 – 474›474Ribulose bisphosphate carboxylase large chainPRO_0000062439Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131N6,N6,N6-trimethyllysineUniRule annotation
    Modified residuei200 – 2001N6-carboxylysineUniRule annotation
    Disulfide bondi246 – 246Interchain; 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

    PRIDEiP48699.

    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

    ProteinModelPortaliP48699.
    SMRiP48699. Positions 17-472.
    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.

    P48699-1 [UniParc]FASTAAdd to Basket

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    SPQXETKASV GFKAGVKDYK LTYYTPDYKT KDTDILAAFR VTPQPGVPPE    50
    EAGAAVAAES STGTWTTVWT DGLTSLDRYK GRCYHIEPVA GEENHFIAYV 100
    AYPLDLFEEG SVTNMFTSIV GNVFGFKALR ALRLEDLRIP PAYSKTFQGP 150
    PHGIQVERDK LNKYGRPLLG CTIKPKLGLS AKNYGRAVYE CLRGGLDFTK 200
    DDENVNSQPF MRWRDRFVFC AEAIYKAQAE TGEIKGHYLN ATAGTCEEMI 250
    KRAVFARELG VPIIMHDYLT GGFTANTSLA HYCRDNGLLL HIHRAMHAVI 300
    DRQKNHGIHF RVLAKALRMS GGDHIHSGTV VGKLEGERDI TLGFVDLLRD 350
    DFIAKDRSRG IYFTQDWVSL PGVLPVASGG IHVWHMPALT EIFGDDSVLQ 400
    FGGGTLGHPW GNAPGAVANR VALEACVQAR NEGRDLAREG NEIIREASKW 450
    SPELAAACEV WKEIKFEFQA VDTL 474
    Length:474
    Mass (Da):52,452
    Last modified:February 1, 1996 - v1
    Checksum:i6E9F94ED90BBDFF3
    GO

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26069 Genomic DNA. Translation: AAB97296.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26069 Genomic DNA. Translation: AAB97296.1 .

    3D structure databases

    ProteinModelPortali P48699.
    SMRi P48699. Positions 17-472.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P48699.

    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. "A comparision of angiosperm phylogenies from nuclear 18S rRNA and rbcL sequences."
      Nickrent D.L., Soltis D.E.
      Ann. Mo. Bot. Gard. 82:208-234(1995)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiRBL_DENCL
    AccessioniPrimary (citable) accession number: P48699
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 69 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