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Q37BZ5

- RBL1A_RHOPS

UniProt

Q37BZ5 - RBL1A_RHOPS

Protein

Ribulose bisphosphate carboxylase large chain 1

Gene

cbbL1

Organism
Rhodopseudomonas palustris (strain BisB5)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (06 Dec 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 sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
    Binding sitei165 – 1651SubstrateUniRule annotation
    Active sitei167 – 1671Proton acceptorUniRule annotation
    Binding sitei169 – 1691SubstrateUniRule annotation
    Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Active sitei286 – 2861Proton acceptorUniRule annotation
    Binding sitei287 – 2871SubstrateUniRule annotation
    Binding sitei319 – 3191SubstrateUniRule annotation
    Sitei326 – 3261Transition state stabilizerUniRule annotation
    Binding sitei371 – 3711SubstrateUniRule 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, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciRPAL316057:GHDC-1575-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain 1UniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunit 1UniRule annotation
    Gene namesi
    Name:cbbL1UniRule annotation
    Ordered Locus Names:RPD_1549
    OrganismiRhodopseudomonas palustris (strain BisB5)
    Taxonomic identifieri316057 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
    ProteomesiUP000001818: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 472472Ribulose bisphosphate carboxylase large chain 1PRO_0000251458Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi316057.RPD_1549.

    Structurei

    3D structure databases

    ProteinModelPortaliQ37BZ5.
    SMRiQ37BZ5. Positions 15-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiMFKRAEY.
    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.

    Q37BZ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKSYQAGVR EYRETYWDPH YTPKDSDILA VFKVIPQAGV PREEAAAAVC    50
    AESSTATWTT VWTDLLTDLD YYKGRAYAIE DVPGDDEAFY AFVAYPMGLF 100
    EEGSIVNVFT SLVGNVFGFK AVRALRLEDV RFPLWFVTTC DGPPHGIQVE 150
    RDKLDKYGRP MLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS 200
    QPFMRWRDRF EFCQEAIEKA EQETGERKGH YLNVTAPNME EIYRRAEFAK 250
    EIGSPIIMSD YLTIGWAAHS SLSRWCRANG MLLHVHRAMH GVIDRNPRHG 300
    INFRVLAKLL RLLGGDHLHS GTVVGKLEGD RAATLGWVDL MRERHVKEDR 350
    SRGLFFDQPW GHMAPVMPVA SGGIHVWHMP ALLAIFGDDA VFQFGGGTLG 400
    HPWGNAAGAA ANRVALEACV RARNEGRDVE REGKDILTAA AQSSPELKVA 450
    METWREIKFE FDVVDKLDAP HR 472
    Length:472
    Mass (Da):53,009
    Last modified:December 6, 2005 - v1
    Checksum:i2C224B243490441D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000283 Genomic DNA. Translation: ABE38786.1.
    RefSeqiWP_011501970.1. NC_007958.1.
    YP_568687.1. NC_007958.1.

    Genome annotation databases

    EnsemblBacteriaiABE38786; ABE38786; RPD_1549.
    GeneIDi4022029.
    KEGGirpd:RPD_1549.
    PATRICi23278049. VBIRhoPal120395_1602.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000283 Genomic DNA. Translation: ABE38786.1 .
    RefSeqi WP_011501970.1. NC_007958.1.
    YP_568687.1. NC_007958.1.

    3D structure databases

    ProteinModelPortali Q37BZ5.
    SMRi Q37BZ5. Positions 15-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 316057.RPD_1549.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE38786 ; ABE38786 ; RPD_1549 .
    GeneIDi 4022029.
    KEGGi rpd:RPD_1549.
    PATRICi 23278049. VBIRhoPal120395_1602.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci RPAL316057:GHDC-1575-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].
      Strain: BisB5.

    Entry informationi

    Entry nameiRBL1A_RHOPS
    AccessioniPrimary (citable) accession number: Q37BZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 57 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