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Q0AHW1

- RBL_NITEC

UniProt

Q0AHW1 - RBL_NITEC

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Nitrosomonas eutropha (strain C91)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      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 sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
    Binding sitei166 – 1661SubstrateUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei170 – 1701SubstrateUniRule annotation
    Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Metal bindingi197 – 1971MagnesiumUniRule annotation
    Active sitei287 – 2871Proton acceptorUniRule annotation
    Binding sitei288 – 2881SubstrateUniRule annotation
    Binding sitei320 – 3201SubstrateUniRule annotation
    Sitei327 – 3271Transition state stabilizerUniRule annotation
    Binding sitei372 – 3721SubstrateUniRule 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

    BioCyciNEUT335283:GHT6-821-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
    Ordered Locus Names:Neut_0804
    OrganismiNitrosomonas eutropha (strain C91)
    Taxonomic identifieri335283 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
    ProteomesiUP000001966: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473Ribulose bisphosphate carboxylase large chainPRO_0000299966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-carboxylysineUniRule annotation

    Proteomic databases

    PRIDEiQ0AHW1.

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

    Protein-protein interaction databases

    STRINGi335283.Neut_0804.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0AHW1.
    SMRiQ0AHW1. Positions 16-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiMETWKEV.
    OrthoDBiEOG6ZKXMS.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01338. RuBisCO_L_type1.
    InterProiIPR020888. 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.

    Sequencei

    Sequence statusi: Complete.

    Q0AHW1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIKTYQAGV KEYRQTYWQP DYVPLDTDIL ACFKITPQSG VDREEAAAAV    50
    AAESSCGTWT TVWTDLLTDL DYYKGRAYRI EDVPGDDARF YAFVAYPIDL 100
    FEEGSVVNVF TSLVGNVFGF KAIRALRLED VRFPIAYVKT CGGPPSGIQV 150
    ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGSL DFTKDDENIN 200
    SQPFMRWRDR FEFVQEATLK AEAETGERKG HYLNVTAPTP EEMYKRAEFA 250
    KEIGAPIIMH DYLAGGLCAN AGLANWCRNN GMLLHVHRAM HAVLDRNPHH 300
    GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFVPED 350
    RSRGIFFDQD WGSMPGAFAV ASGGIHVWHM PALVAIFGDD SVLQFGGGTL 400
    GHPWGNAAGA HANRVALEAC VQARNEGRQI EKEGREILTA AAQHSPELKI 450
    AMETWKEIKF EFDTVDKLDI AHK 473
    Length:473
    Mass (Da):52,688
    Last modified:October 17, 2006 - v1
    Checksum:i0E1D9FEAF68426BC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000450 Genomic DNA. Translation: ABI59071.1.
    RefSeqiWP_011633896.1. NC_008344.1.
    YP_747036.1. NC_008344.1.

    Genome annotation databases

    EnsemblBacteriaiABI59071; ABI59071; Neut_0804.
    GeneIDi4272958.
    KEGGinet:Neut_0804.
    PATRICi22718721. VBINitEut7577_1030.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000450 Genomic DNA. Translation: ABI59071.1 .
    RefSeqi WP_011633896.1. NC_008344.1.
    YP_747036.1. NC_008344.1.

    3D structure databases

    ProteinModelPortali Q0AHW1.
    SMRi Q0AHW1. Positions 16-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 335283.Neut_0804.

    Proteomic databases

    PRIDEi Q0AHW1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABI59071 ; ABI59071 ; Neut_0804 .
    GeneIDi 4272958.
    KEGGi net:Neut_0804.
    PATRICi 22718721. VBINitEut7577_1030.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NEUT335283:GHT6-821-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 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.
    ProtoNeti Search...

    Publicationsi

    1. "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
      Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
      Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C91.

    Entry informationi

    Entry nameiRBL_NITEC
    AccessioniPrimary (citable) accession number: Q0AHW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 55 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3