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Q3SNG2

- RBL1B_NITWN

UniProt

Q3SNG2 - RBL1B_NITWN

Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      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 sitei128 – 1281Substrate; in homodimeric partnerUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Active sitei180 – 1801Proton acceptorUniRule annotation
    Binding sitei182 – 1821SubstrateUniRule annotation
    Metal bindingi206 – 2061Magnesium; via carbamate groupUniRule annotation
    Metal bindingi208 – 2081MagnesiumUniRule annotation
    Metal bindingi209 – 2091MagnesiumUniRule annotation
    Active sitei298 – 2981Proton acceptorUniRule annotation
    Binding sitei299 – 2991SubstrateUniRule annotation
    Binding sitei331 – 3311SubstrateUniRule annotation
    Sitei338 – 3381Transition state stabilizerUniRule annotation
    Binding sitei383 – 3831SubstrateUniRule 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

    BioCyciNWIN323098:GJEG-2980-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain 2UniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunit 2UniRule annotation
    Gene namesi
    Name:cbbL2UniRule annotation
    Ordered Locus Names:Nwi_2929
    OrganismiNitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
    Taxonomic identifieri323098 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
    ProteomesiUP000002531: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 489489Ribulose bisphosphate carboxylase large chain 2PRO_0000251452Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei206 – 2061N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi323098.Nwi_2929.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3SNG2.
    SMRiQ3SNG2. Positions 26-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiCTPLKQA.
    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.

    Q3SNG2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVQNEKSMT VRGKDRYKSG VMSYKKMGYW EPDYTPKDTD VICLFRVTPQ    50
    DGVDPIEASA AVAGESSTAT WTVVWTDRLT AAEKYRAKCY RVDPVPGAEG 100
    QYFAYIAYDL DLFEPGSISN LTASVIGNVF GFKPLKALRL EDMRLPVAYV 150
    KTFKGPPTGI VVERERLDKF GRPLLGATVK PKLGLSGRNY GRVVYEALKG 200
    GLDFTKDDEN INSQPFMHWR ERFLYCMEAV NRAQAATGEI KGSYLNVTAA 250
    TMEDMYERAE FAKELGSVVV MIDLVIGYTA IQSMSNWARK NDMILHLHRA 300
    GHSTYTRQRS HGVSFRVISK WMRLAGVDHI HAGTVVGKLE GDPLTTRGFY 350
    DICREEYNPT QLEHGIFFDQ NWASLNKVMP VASGGIHAGQ MHQLIQHLGE 400
    DVVLQFGGGT IGHPMGIQAG ATANRVALEA MILARNEGRD YVSEGPEILA 450
    KAAASCTPLK QALEVWKDVT FDYASTDAPD YVPTAVPAA 489
    Length:489
    Mass (Da):54,148
    Last modified:October 11, 2005 - v1
    Checksum:iE7A0458BCD485A9E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000115 Genomic DNA. Translation: ABA06179.1.
    RefSeqiYP_319531.1. NC_007406.1.

    Genome annotation databases

    EnsemblBacteriaiABA06179; ABA06179; Nwi_2929.
    GeneIDi3674284.
    KEGGinwi:Nwi_2929.
    PATRICi22702997. VBINitWin102302_3305.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000115 Genomic DNA. Translation: ABA06179.1 .
    RefSeqi YP_319531.1. NC_007406.1.

    3D structure databases

    ProteinModelPortali Q3SNG2.
    SMRi Q3SNG2. Positions 26-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 323098.Nwi_2929.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABA06179 ; ABA06179 ; Nwi_2929 .
    GeneIDi 3674284.
    KEGGi nwi:Nwi_2929.
    PATRICi 22702997. VBINitWin102302_3305.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NWIN323098:GJEG-2980-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. "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
      Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
      Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Nb-255 / ATCC 25391.

    Entry informationi

    Entry nameiRBL1B_NITWN
    AccessioniPrimary (citable) accession number: Q3SNG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 56 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3