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F7US61

- F7US61_SYNYG

UniProt

F7US61 - F7US61_SYNYG

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechocystis sp. (strain PCC 6803 / GT-S)
Status
Unreviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 25 (01 Oct 2014)
      Sequence version 1 (21 Sep 2011)
      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, PhotosynthesisUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciSSP1148:GJOT-2263-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:SYNGTS_2225Imported
    OrganismiSynechocystis sp. (strain PCC 6803 / GT-S)Imported
    Taxonomic identifieri1111707 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    ProteomesiUP000008187: 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

    PRIDEiF7US61.

    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

    ProteinModelPortaliF7US61.
    SMRiF7US61. 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.

    F7US61-1 [UniParc]FASTAAdd to Basket

    « Hide

    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:September 21, 2011 - v1
    Checksum:i45B9322482745B2B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012205 Genomic DNA. Translation: BAK50973.1.
    RefSeqiNP_442120.1. NC_000911.1.
    YP_005652178.1. NC_017277.1.
    YP_007451997.1. NC_020286.1.

    Genome annotation databases

    EnsemblBacteriaiBAK50973; BAK50973; SYNGTS_2225.
    GeneIDi952593.
    KEGGisyn:slr0009.
    syy:SYNGTS_2225.
    syz:MYO_122490.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP012205 Genomic DNA. Translation: BAK50973.1 .
    RefSeqi NP_442120.1. NC_000911.1.
    YP_005652178.1. NC_017277.1.
    YP_007451997.1. NC_020286.1.

    3D structure databases

    ProteinModelPortali F7US61.
    SMRi F7US61. Positions 6-464.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi F7US61.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAK50973 ; BAK50973 ; SYNGTS_2225 .
    GeneIDi 952593.
    KEGGi syn:slr0009.
    syy:SYNGTS_2225.
    syz:MYO_122490.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci SSP1148:GJOT-2263-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. "Genomic structure of the cyanobacterium Synechocystis sp. PCC 6803 strain GT-S."
      Tajima N., Sato S., Maruyama F., Kaneko T., Sasaki N.V., Kurokawa K., Ohta H., Kanesaki Y., Yoshikawa H., Tabata S., Ikeuchi M., Sato N.
      DNA Res. 18:393-399(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 6803 / GT-SImported.

    Entry informationi

    Entry nameiF7US61_SYNYG
    AccessioniPrimary (citable) accession number: F7US61
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 21, 2011
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 25 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