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O84917

- RBL2_THIK1

UniProt

O84917 - RBL2_THIK1

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Thiomonas intermedia (strain K12) (Thiobacillus intermedius)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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. 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 sitei113 – 1131Substrate; in homodimeric partnerUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei170 – 1701SubstrateUniRule annotation
    Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Active sitei289 – 2891Proton acceptorUniRule annotation
    Binding sitei290 – 2901SubstrateUniRule annotation
    Binding sitei323 – 3231SubstrateUniRule annotation
    Sitei331 – 3311Transition state stabilizerUniRule annotation
    Binding sitei370 – 3701SubstrateUniRule 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. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciTINT75379:GH6C-1675-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCOUniRule annotation
    Gene namesi
    Name:cbbMUniRule annotation
    Ordered Locus Names:Tint_1655
    OrganismiThiomonas intermedia (strain K12) (Thiobacillus intermedius)
    Taxonomic identifieri75379 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesThiomonas
    ProteomesiUP000002185: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Ribulose bisphosphate carboxylasePRO_0000062669Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliO84917.
    SMRiO84917. Positions 4-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000230831.
    KOiK01601.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01339. RuBisCO_L_type2.
    InterProiIPR020871. RuBisCO.
    IPR020878. RuBisCo_large_chain_AS.
    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.

    O84917-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE    50
    SSTGTNVEVS TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR 100
    FMIVSFLTLV IGNNQGMGDV EYGKMIDFYV PERAIQMFDG PATDISNLWR 150
    ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ AAYQFWLGGD FIKNDEPQGN 200
    QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH EMCARADFAL 250
    EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS 300
    SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC 350
    QGPVYFQKWY GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG 400
    HIDSPAAGAK SLRQAYECWK AGADPIEYAK EHKEFARAFE SFPGDADKLF 450
    PGWRDKLGVH K 461
    Length:461
    Mass (Da):50,818
    Last modified:November 1, 1998 - v1
    Checksum:iD470D17F356800E2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012127 Genomic DNA. Translation: AAC24964.1.
    CP002021 Genomic DNA. Translation: ADG31025.1.
    RefSeqiWP_013123277.1. NC_014153.1.
    YP_003643355.1. NC_014153.1.

    Genome annotation databases

    EnsemblBacteriaiADG31025; ADG31025; Tint_1655.
    GeneIDi9152388.
    KEGGitin:Tint_1655.
    PATRICi38293853. VBIThiInt85915_1685.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012127 Genomic DNA. Translation: AAC24964.1 .
    CP002021 Genomic DNA. Translation: ADG31025.1 .
    RefSeqi WP_013123277.1. NC_014153.1.
    YP_003643355.1. NC_014153.1.

    3D structure databases

    ProteinModelPortali O84917.
    SMRi O84917. Positions 4-459.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADG31025 ; ADG31025 ; Tint_1655 .
    GeneIDi 9152388.
    KEGGi tin:Tint_1655.
    PATRICi 38293853. VBIThiInt85915_1685.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.

    Enzyme and pathway databases

    BioCyci TINT75379:GH6C-1675-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01339. RuBisCO_L_type2.
    InterProi IPR020871. RuBisCO.
    IPR020878. RuBisCo_large_chain_AS.
    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 form II Rubisco gene and associated genes in Thiobacillus intermedius."
      Shively J.M., Soyer F.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    3. "Cloning and expression of the D-ribulose-1,5-bisphosphate carboxylase/oxygenase form II gene from Thiobacillus intermedius in Escherichia coli."
      Stoner M.T., Shively J.M.
      FEMS Microbiol. Lett. 107:287-292(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: EXPRESSION IN T.INTERMEDIUS.
    4. Shively J.M.
      Unpublished observations (OCT-2005)
      Cited for: PROBABLE EXPRESSION.

    Entry informationi

    Entry nameiRBL2_THIK1
    AccessioniPrimary (citable) accession number: O84917
    Secondary accession number(s): D5X1M9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 73 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 contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits.UniRule annotation

    Caution

    No expression of this protein has been seen during autotrophic and mixotrophic growth, however the protein is probably expressed under other conditions. In a related bacteria (T.neapolitanus) expression has been seen when the form I enzyme has been knocked out.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3