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Q8DIS5

- RBL_THEEB

UniProt

Q8DIS5 - RBL_THEEB

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 sitei123 – 1231Substrate; in homodimeric partnerUniRule annotation
    Binding sitei173 – 1731SubstrateUniRule annotation
    Active sitei175 – 1751Proton acceptorUniRule annotation
    Binding sitei177 – 1771SubstrateUniRule annotation
    Metal bindingi201 – 2011Magnesium; via carbamate groupUniRule annotation
    Metal bindingi203 – 2031MagnesiumUniRule annotation
    Metal bindingi204 – 2041MagnesiumUniRule annotation
    Active sitei294 – 2941Proton acceptorUniRule annotation
    Binding sitei295 – 2951SubstrateUniRule annotation
    Binding sitei327 – 3271SubstrateUniRule annotation
    Sitei334 – 3341Transition state stabilizerUniRule annotation
    Binding sitei379 – 3791SubstrateUniRule 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

    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:tll1506
    OrganismiThermosynechococcus elongatus (strain BP-1)
    Taxonomic identifieri197221 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
    ProteomesiUP000000440: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 475475Ribulose bisphosphate carboxylase large chainPRO_0000062649Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei201 – 2011N6-carboxylysineUniRule annotation
    Disulfide bondi247 – 247Interchain; 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

    PRIDEiQ8DIS5.

    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

    STRINGi197221.tll1506.

    Structurei

    Secondary structure

    1
    475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 244
    Beta strandi35 – 4410
    Helixi50 – 6011
    Turni61 – 633
    Beta strandi66 – 683
    Helixi70 – 745
    Helixi77 – 804
    Beta strandi83 – 897
    Beta strandi93 – 953
    Beta strandi97 – 1037
    Helixi105 – 1073
    Helixi113 – 1219
    Helixi124 – 1263
    Beta strandi130 – 13910
    Helixi142 – 1454
    Helixi155 – 1628
    Beta strandi169 – 1735
    Beta strandi175 – 1784
    Helixi182 – 19413
    Beta strandi198 – 2014
    Beta strandi207 – 2093
    Helixi214 – 23219
    Beta strandi237 – 2415
    Helixi247 – 25913
    Beta strandi263 – 2686
    Helixi269 – 2724
    Helixi274 – 28714
    Beta strandi290 – 2945
    Helixi298 – 3025
    Beta strandi305 – 3095
    Helixi311 – 32111
    Beta strandi324 – 3274
    Beta strandi331 – 3355
    Helixi339 – 35012
    Beta strandi352 – 3543
    Helixi358 – 3603
    Beta strandi375 – 3817
    Helixi384 – 3863
    Helixi387 – 3948
    Beta strandi396 – 4016
    Helixi404 – 4074
    Helixi413 – 43119
    Turni432 – 4343
    Turni437 – 4393
    Helixi441 – 45111
    Helixi453 – 46210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YBVX-ray2.30A/C/E/G/I/K/M/O1-475[»]
    3ZXWX-ray2.10A/C/E/G1-475[»]
    ProteinModelPortaliQ8DIS5.
    SMRiQ8DIS5. Positions 12-475.
    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.

    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.

    Q8DIS5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAYTQSKSQK VGYQAGVKDY RLTYYTPDYT PKDTDILAAF RVTPQPGVPF    50
    EEAAAAVAAE SSTGTWTTVW TDLLTDLDRY KGCCYDIEPL PGEDNQFIAY 100
    IAYPLDLFEE GSVTNMLTSI VGNVFGFKAL KALRLEDLRI PVAYLKTFQG 150
    PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
    KDDENINSQP FQRWRDRFLF VADAIHKAQA ETGEIKGHYL NVTAPTCEEM 250
    LKRAEFAKEL EMPIIMHDFL TAGFTANTTL SKWCRDNGML LHIHRAMHAV 300
    MDRQKNHGIH FRVLAKCLRM SGGDHIHTGT VVGKLEGDKA VTLGFVDLLR 350
    ENYIEQDRSR GIYFTQDWAS MPGVMAVASG GIHVWHMPAL VDIFGDDAVL 400
    QFGGGTLGHP WGNAPGATAN RVALEACIQA RNEGRDLMRE GGDIIREAAR 450
    WSPELAAACE LWKEIKFEFE AQDTI 475
    Length:475
    Mass (Da):53,025
    Last modified:March 1, 2003 - v1
    Checksum:iB4A97CD4D6A3EB91
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC09058.1.
    RefSeqiNP_682296.1. NC_004113.1.
    WP_011057346.1. NC_004113.1.

    Genome annotation databases

    EnsemblBacteriaiBAC09058; BAC09058; BAC09058.
    GeneIDi1011208.
    KEGGitel:tll1506.
    PATRICi23928370. VBITheElo119873_1580.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC09058.1 .
    RefSeqi NP_682296.1. NC_004113.1.
    WP_011057346.1. NC_004113.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YBV X-ray 2.30 A/C/E/G/I/K/M/O 1-475 [» ]
    3ZXW X-ray 2.10 A/C/E/G 1-475 [» ]
    ProteinModelPortali Q8DIS5.
    SMRi Q8DIS5. Positions 12-475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 197221.tll1506.

    Proteomic databases

    PRIDEi Q8DIS5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC09058 ; BAC09058 ; BAC09058 .
    GeneIDi 1011208.
    KEGGi tel:tll1506.
    PATRICi 23928370. VBITheElo119873_1580.

    Phylogenomic databases

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

    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: BP-1.

    Entry informationi

    Entry nameiRBL_THEEB
    AccessioniPrimary (citable) accession number: Q8DIS5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 75 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3