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G9AH13

- G9AH13_RHIFH

UniProt

G9AH13 - G9AH13_RHIFH

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Rhizobium fredii (strain HH103) (Sinorhizobium fredii)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 21 (01 Oct 2014)
      Sequence version 1 (22 Feb 2012)
      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

    LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciSFRE1117943:GJT5-5040-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 annotationImported
    Ordered Locus Names:SFHH103_05883Imported
    Encoded oniPlasmid pSfHH103eImported
    OrganismiRhizobium fredii (strain HH103) (Sinorhizobium fredii)Imported
    Taxonomic identifieri1117943 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
    ProteomesiUP000007735: Plasmid pSfHH103e

    PTM / Processingi

    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

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01601.

    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.

    G9AH13-1 [UniParc]FASTAAdd to Basket

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    MNADAKTEIK GKERYRAGVL KYAQMGYWNG DYEPKDTDLI ALFRITPQEG    50
    VDPIEAAAAV AGESSTATWT VVWTDRLTAC DQYRAKAYRV DPVPGTPGQY 100
    FCYVAYDLIL FEEGSIANLT ASIIGNVFSF KPLKAARLED MRLPVAYVKT 150
    FKGPPTGIVV ERERLDKFGK PLLGATTKPK LGLSGKNYGR VVYEGLKGGL 200
    DFMKDDENIN SQPFMHWRDR YLYCMDAVNH ASAVTGEVKG HYLNITAGTM 250
    EEMYRRAEFA KELGSVIVMV DLIIGWTAIQ SISEWCRQND MILHMHRAGH 300
    GTYTRQKNHG ISFRVIAKWL RLAGVDHLHA GTAVGKLEGD PMTVQGYYNV 350
    CREMRNKIDL PRGLFFEQDW ADIKKVMPVA SGGIHAGQMH QLLDLFGDDV 400
    VLQFGGGTIG HPMGIQAGAT ANRVALEAMV LARNEGRDIA HEGPEILRAA 450
    AKWCKPLEAA LDTWGNISFN YTPTDSSDFV PSVSVA 486
    Length:486
    Mass (Da):53,841
    Last modified:February 22, 2012 - v1
    Checksum:i12A5226E9AF838A8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    HE616899 Genomic DNA. Translation: CCF00345.1.
    RefSeqiWP_014331997.1. NC_016815.1.
    YP_005192484.1. NC_016815.1.

    Genome annotation databases

    EnsemblBacteriaiCCF00345; CCF00345; SFHH103_05883.
    GeneIDi11800073.
    KEGGisfh:SFHH103_05883.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    HE616899 Genomic DNA. Translation: CCF00345.1 .
    RefSeqi WP_014331997.1. NC_016815.1.
    YP_005192484.1. NC_016815.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCF00345 ; CCF00345 ; SFHH103_05883 .
    GeneIDi 11800073.
    KEGGi sfh:SFHH103_05883.

    Phylogenomic databases

    KOi K01601.

    Enzyme and pathway databases

    BioCyci SFRE1117943:GJT5-5040-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiG9AH13_RHIFH
    AccessioniPrimary (citable) accession number: G9AH13
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 22, 2012
    Last sequence update: February 22, 2012
    Last modified: October 1, 2014
    This is version 21 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    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 proteomeImported, PlasmidImported

    External Data

    Dasty 3