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H0PB08

- H0PB08_9SYNC

UniProt

H0PB08 - H0PB08_9SYNC

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Synechocystis sp. PCC 6803 substr. PCC-N
Status
Unreviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 22 (01 Oct 2014)
      Sequence version 1 (22 Feb 2012)
      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 sitei118 – 1181Substrate; in homodimeric partnerUniRule annotation
    Binding sitei168 – 1681SubstrateUniRule annotation
    Active sitei170 – 1701Proton acceptorUniRule annotation
    Binding sitei172 – 1721SubstrateUniRule annotation
    Metal bindingi196 – 1961Magnesium; via carbamate groupUniRule annotation
    Metal bindingi198 – 1981MagnesiumUniRule annotation
    Metal bindingi199 – 1991MagnesiumUniRule annotation
    Active sitei289 – 2891Proton acceptorUniRule annotation
    Binding sitei290 – 2901SubstrateUniRule annotation
    Binding sitei322 – 3221SubstrateUniRule annotation
    Sitei329 – 3291Transition state stabilizerUniRule annotation
    Binding sitei374 – 3741SubstrateUniRule 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

    LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciSSP1080229:GLM2-2255-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:rbcLUniRule annotation
    Synonyms:cbbLUniRule annotation
    ORF Names:SYNPCCN_2223Imported
    OrganismiSynechocystis sp. PCC 6803 substr. PCC-NImported
    Taxonomic identifieri1080229 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    ProteomesiUP000007108: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei196 – 1961N6-carboxylysineUniRule annotation
    Disulfide bondi242 – 242Interchain; 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 bondUniRule annotation

    Proteomic databases

    PRIDEiH0PB08.

    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

    ProteinModelPortaliH0PB08.
    SMRiH0PB08. Positions 6-464.
    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.

    H0PB08-1 [UniParc]FASTAAdd to Basket

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    MVQAKAGFKA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPAEEAAA    50
    AVAAESSTGT WTTVWTDNLT DLDRYKGRCY DLEAVPNEDN QYFAFIAYPL 100
    DLFEEGSVTN VLTSLVGNVF GFKALRALRL EDIRFPVALI KTFQGPPHGI 150
    TVERDKLNKY GRPLLGCTIK PKLGLSAKNY GRAVYECLRG GLDFTKDDEN 200
    INSQPFMRWR DRFLFVQEAI EKAQAETNEM KGHYLNVTAG TCEEMMKRAE 250
    FAKEIGTPII MHDFFTGGFT ANTTLARWCR DNGILLHIHR AMHAVVDRQK 300
    NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGERGITMGF VDLMREDYVE 350
    EDRSRGIFFT QDYASMPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG 400
    TLGHPWGNAP GATANRVALE ACVQARNEGR NLAREGNDVI REACRWSPEL 450
    AAACELWKEI KFEFEAMDTL 470
    Length:470
    Mass (Da):52,491
    Last modified:February 22, 2012 - v1
    Checksum:i45B9322482745B2B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012277 Genomic DNA. Translation: BAL33140.1.
    RefSeqiYP_005409862.1. NC_017052.1.

    Genome annotation databases

    EnsemblBacteriaiBAL33140; BAL33140; SYNPCCN_2223.
    GeneIDi12011000.
    KEGGisys:SYNPCCN_2223.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012277 Genomic DNA. Translation: BAL33140.1 .
    RefSeqi YP_005409862.1. NC_017052.1.

    3D structure databases

    ProteinModelPortali H0PB08.
    SMRi H0PB08. Positions 6-464.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi H0PB08.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAL33140 ; BAL33140 ; SYNPCCN_2223 .
    GeneIDi 12011000.
    KEGGi sys:SYNPCCN_2223.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci SSP1080229:GLM2-2255-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. "Identification of substrain-specific mutations by massively parallel whole-genome resequencing of Synechocystis sp. PCC 6803."
      Kanesaki Y., Shiwa Y., Tajima N., Suzuki M., Watanabe S., Sato N., Ikeuchi M., Yoshikawa H.
      DNA Res. 19:67-79(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiH0PB08_9SYNC
    AccessioniPrimary (citable) accession number: H0PB08
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 22, 2012
    Last sequence update: February 22, 2012
    Last modified: October 1, 2014
    This is version 22 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    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 proteomeImported

    External Data

    Dasty 3