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P56889

- RBL1_SINMW

UniProt

P56889 - RBL1_SINMW

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      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 sitei126 – 1261Substrate; in homodimeric partnerUniRule annotation
    Binding sitei176 – 1761SubstrateUniRule annotation
    Active sitei178 – 1781Proton acceptorUniRule annotation
    Binding sitei180 – 1801SubstrateUniRule annotation
    Metal bindingi204 – 2041Magnesium; via carbamate groupUniRule annotation
    Metal bindingi206 – 2061MagnesiumUniRule annotation
    Metal bindingi207 – 2071MagnesiumUniRule annotation
    Active sitei296 – 2961Proton acceptorUniRule annotation
    Binding sitei297 – 2971SubstrateUniRule annotation
    Binding sitei329 – 3291SubstrateUniRule annotation
    Sitei336 – 3361Transition state stabilizerUniRule annotation
    Binding sitei381 – 3811SubstrateUniRule 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

    BioCyciSMED366394:GJAL-3985-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:Smed_3924
    Encoded oniPlasmid pSMED010 Publication
    OrganismiSinorhizobium medicae (strain WSM419) (Ensifer medicae)
    Taxonomic identifieri366394 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
    ProteomesiUP000001108: Plasmid pSMED01

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Ribulose bisphosphate carboxylase large chainPRO_0000062644Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei204 – 2041N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi366394.Smed_3924.

    Structurei

    3D structure databases

    ProteinModelPortaliP56889.
    SMRiP56889. Positions 7-480.
    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.

    P56889-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNADAKTEIK GRERYKAGVL KYAQMGYWNG DYEPKDTDLI ALFRITPQDG    50
    VDPIEAAAAV AGESSTATWT VVWTDRLTAC DQYRAKAYRV DPVPGTPGQY 100
    FCYVAYDLIL FEEGSIANLT ASIIGNVFSF KPLKAARLED MRLPVAYVKT 150
    FKGPPTGIVV ERERLDKFGK PLLGATTKPK LGLSGKNYGR VVYEGLKGGL 200
    DFMKDDENIN SQPFMHWRDR YLYCMEAVNH ASAVTGEVKG HYLNVTAGTM 250
    EEMYRRAEFA KELGSVIVMV DLIIGWTAIQ SMSEWCRQND MILHMHRAGH 300
    GTYTRQKNHG ISFRVIAKWL RLAGVDHLHA GTAVGKLEGD PLTVQGYYNV 350
    CREMKNAVDL PRGLFFEQDW ADLKKVLPVA SGGIHAGQMH QLLDLFGDDV 400
    VLQFGGGTIG HPMGIQAGAT ANRVALEAMV LARNEGRDIA HEGPEILRAA 450
    AKWCKPLEAA LDTWGNISFN YTPTDTSDFV PSVTAA 486
    Length:486
    Mass (Da):53,709
    Last modified:November 13, 2007 - v2
    Checksum:iCF54E04F5FD76336
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61K → N in AAF25379. 1 PublicationCurated
    Sequence conflicti35 – 351K → N in AAF25379. 1 PublicationCurated
    Sequence conflicti52 – 521D → H in AAF25379. 1 PublicationCurated
    Sequence conflicti56 – 561A → P in AAF25379. 1 PublicationCurated
    Sequence conflicti76 – 761R → P in AAF25379. 1 PublicationCurated
    Sequence conflicti128 – 1281F → L in AAF25379. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF211846 Genomic DNA. Translation: AAF25379.1.
    CP000739 Genomic DNA. Translation: ABR62734.1.
    RefSeqiYP_001312667.1. NC_009620.1.

    Genome annotation databases

    EnsemblBacteriaiABR62734; ABR62734; Smed_3924.
    GeneIDi5318709.
    KEGGismd:Smed_3924.
    PATRICi23613394. VBISinMed134228_0370.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF211846 Genomic DNA. Translation: AAF25379.1 .
    CP000739 Genomic DNA. Translation: ABR62734.1 .
    RefSeqi YP_001312667.1. NC_009620.1.

    3D structure databases

    ProteinModelPortali P56889.
    SMRi P56889. Positions 7-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 366394.Smed_3924.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR62734 ; ABR62734 ; Smed_3924 .
    GeneIDi 5318709.
    KEGGi smd:Smed_3924.
    PATRICi 23613394. VBISinMed134228_0370.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SMED366394:GJAL-3985-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. "Genetic regulation of C1 metabolism in Sinorhizobium meliloti."
      Fenner B.J., Tiwari R.P., Dilworth M.J.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: WSM419.

    Entry informationi

    Entry nameiRBL1_SINMW
    AccessioniPrimary (citable) accession number: P56889
    Secondary accession number(s): A6UGF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 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, Plasmid

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3