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P42721

- RBL1P_CUPNH

UniProt

P42721 - RBL1P_CUPNH

Protein

Ribulose bisphosphate carboxylase large chain, plasmid

Gene

cbbL2

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (04 Jan 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.

    Catalytic activityi

    2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei126 – 1261Substrate; in homodimeric partnerBy similarity
    Binding sitei176 – 1761SubstrateBy similarity
    Active sitei178 – 1781Proton acceptorBy similarity
    Binding sitei180 – 1801SubstrateBy similarity
    Metal bindingi204 – 2041Magnesium; via carbamate groupBy similarity
    Metal bindingi206 – 2061MagnesiumBy similarity
    Metal bindingi207 – 2071MagnesiumBy similarity
    Active sitei296 – 2961Proton acceptorBy similarity
    Binding sitei297 – 2971SubstrateBy similarity
    Binding sitei329 – 3291SubstrateBy similarity
    Sitei336 – 3361Transition state stabilizerBy similarity
    Binding sitei381 – 3811SubstrateBy similarity

    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

    BioCyciCNEC381666:GJUJ-6701-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain, plasmid (EC:4.1.1.39)
    Short name:
    RuBisCO large subunit
    Gene namesi
    Name:cbbL2
    Synonyms:cbbL, cbxLP, cfxLP
    Ordered Locus Names:PHG427
    Encoded oniPlasmid megaplasmid pHG10 Publication
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000008210: Plasmid megaplasmid pHG1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Ribulose bisphosphate carboxylase large chain, plasmidPRO_0000062642Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei204 – 2041N6-carboxylysineBy similarity

    Expressioni

    Inductioni

    Total RuBisCO activity (both chromosome and plasmid-derived enzyme) is high under lithoautotrophic growth conditions, intermediate when grown on fructose and poor when grown on pyruvate.

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains.By similarity

    Protein-protein interaction databases

    STRINGi381666.PHG427.

    Structurei

    3D structure databases

    ProteinModelPortaliP42721.
    SMRiP42721. Positions 24-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    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.

    P42721-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAPESVQAK PRKRYDAGVM KYKEMGYWDG DYEPKDTDLL ALFRITPQDG    50
    VDPVEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF 100
    FCYVAYDLSL FEEGSIANLT ASIIGNVFSF KPIKAARLED MRFPVAYVKT 150
    FAGPSTGIIV ERERLDKFGR PLLGATTKPK LGLSGRNYGR VVYEGLKGGL 200
    DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG SYLNVTAGTM 250
    EEMYRRAEFA KSLGSVVIMI DLIVGWTCIQ SMSNWCRQND MILHLHRAGH 300
    GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV 350
    CRDAYTHTDL TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV 400
    VLQFGGGTIG HPQGIQAGAT ANRVALEAMV LARNEGRDIL NEGPEILRDA 450
    ARWCGPLRAA LDTWGDISFN YTPTDTSDFA PTASVA 486
    Length:486
    Mass (Da):53,809
    Last modified:January 4, 2005 - v3
    Checksum:i38443E663E0EEE13
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti198 – 1981G → R in AAA83747. (PubMed:7543477)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20585 Genomic DNA. Translation: AAA83747.1.
    AY305378 Genomic DNA. Translation: AAP86176.1.
    M65064 Genomic DNA. Translation: AAA21980.1.
    PIRiI39559.
    RefSeqiNP_943062.1. NC_005241.1.
    WP_011154339.1. NC_005241.1.

    Genome annotation databases

    EnsemblBacteriaiAAP86176; AAP86176; PHG427.
    GeneIDi2656546.
    KEGGireh:PHG427.
    PATRICi35229366. VBIRalEut6770_0355.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20585 Genomic DNA. Translation: AAA83747.1 .
    AY305378 Genomic DNA. Translation: AAP86176.1 .
    M65064 Genomic DNA. Translation: AAA21980.1 .
    PIRi I39559.
    RefSeqi NP_943062.1. NC_005241.1.
    WP_011154339.1. NC_005241.1.

    3D structure databases

    ProteinModelPortali P42721.
    SMRi P42721. Positions 24-467.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 381666.PHG427.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP86176 ; AAP86176 ; PHG427 .
    GeneIDi 2656546.
    KEGGi reh:PHG427.
    PATRICi 35229366. VBIRalEut6770_0355.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CNEC381666:GJUJ-6701-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. "Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase genes and cbb promoters of Alcaligenes eutrophus."
      Kusian B., Bednarski R., Husemann M., Bowien B.
      J. Bacteriol. 177:4442-4450(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION UNDER DIFFERENT GROWTH CONDITIONS.
    2. "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."
      Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.
      J. Mol. Biol. 332:369-383(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
    3. "Identification of cfxR, an activator gene of autotrophic CO2 fixation in Alcaligenes eutrophus."
      Windhoevel U., Bowien B.
      Mol. Microbiol. 5:2695-2705(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.

    Entry informationi

    Entry nameiRBL1P_CUPNH
    AccessioniPrimary (citable) accession number: P42721
    Secondary accession number(s): Q7WWS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 97 of the entry and version 3 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" By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Plasmid, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3