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B2J8T2

- RBL_NOSP7

UniProt

B2J8T2 - RBL_NOSP7

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      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 sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
    Binding sitei174 – 1741SubstrateUniRule annotation
    Active sitei176 – 1761Proton acceptorUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
    Metal bindingi204 – 2041MagnesiumUniRule annotation
    Metal bindingi205 – 2051MagnesiumUniRule annotation
    Active sitei295 – 2951Proton acceptorUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Sitei335 – 3351Transition state stabilizerUniRule annotation
    Binding sitei380 – 3801SubstrateUniRule 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

    Enzyme and pathway databases

    BioCyciNPUN63737:GJNP-4063-MONOMER.

    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:cbbLUniRule annotation
    Synonyms:rbcLUniRule annotation
    Ordered Locus Names:Npun_F4195
    OrganismiNostoc punctiforme (strain ATCC 29133 / PCC 73102)
    Taxonomic identifieri63737 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
    ProteomesiUP000001191: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 476476Ribulose bisphosphate carboxylase large chainPRO_1000142750Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-carboxylysineUniRule annotation
    Disulfide bondi248 – 248Interchain; 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

    Proteomic databases

    PRIDEiB2J8T2.

    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

    Protein-protein interaction databases

    STRINGi63737.Npun_F4195.

    Structurei

    3D structure databases

    ProteinModelPortaliB2J8T2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.
    OrthoDBiEOG6ZKXMS.
    PhylomeDBiB2J8T2.

    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.

    B2J8T2-1 [UniParc]FASTAAdd to Basket

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    MSYAQTKTQS KSGYQAGVKD YRLTYYTPDY TPKDTDLLAA FRMTPQPGVP    50
    PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQYIC 100
    YVAYPLDLFE EGSVTNVLTS IVGNVFGFKA LRALRLEDIR FPVAYIKTFQ 150
    GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
    TKDDENINSA PFQRWRDRFL FVAEAINKAQ AETGEIKGHY LNVTAPTCEQ 250
    MLQRAEYAKE LKQPIIMHDY LTAGFTANTT LARWCRDNGI LLHIHRAMHA 300
    VIDRQKNHGI HFRVLAKALR LSGGDHIHTG TVVGKLEGER GITMGFVDLL 350
    RENYIEQDKS RGIYFTQDWA SLPGVMAVAS GGIHVWHMPA LVEIFGDDSV 400
    LQFGGGTLGH PWGNAPGATA NRVALEAVVQ ARNEGRNLAR EGNDIIREAA 450
    KWSPELAVAC ELWKEIKFEF EAMDTV 476
    Length:476
    Mass (Da):53,083
    Last modified:June 10, 2008 - v1
    Checksum:i1D19758D23068D33
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001037 Genomic DNA. Translation: ACC82570.1.
    RefSeqiYP_001867513.1. NC_010628.1.

    Genome annotation databases

    EnsemblBacteriaiACC82570; ACC82570; Npun_F4195.
    GeneIDi6253539.
    KEGGinpu:Npun_F4195.
    PATRICi22761530. VBINosPun48114_4924.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001037 Genomic DNA. Translation: ACC82570.1 .
    RefSeqi YP_001867513.1. NC_010628.1.

    3D structure databases

    ProteinModelPortali B2J8T2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 63737.Npun_F4195.

    Proteomic databases

    PRIDEi B2J8T2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACC82570 ; ACC82570 ; Npun_F4195 .
    GeneIDi 6253539.
    KEGGi npu:Npun_F4195.
    PATRICi 22761530. VBINosPun48114_4924.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi FTQDWAS.
    OrthoDBi EOG6ZKXMS.
    PhylomeDBi B2J8T2.

    Enzyme and pathway databases

    BioCyci NPUN63737:GJNP-4063-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29133 / PCC 73102.

    Entry informationi

    Entry nameiRBL_NOSP7
    AccessioniPrimary (citable) accession number: B2J8T2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 37 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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