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Q31IK0

- RBL1A_THICR

UniProt

Q31IK0 - RBL1A_THICR

Protein

Ribulose bisphosphate carboxylase large chain 1

Gene

cbbL1

Organism
Thiomicrospira crunogena (strain XCL-2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (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

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciTCRU317025:GHE8-433-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:Tcr_0427
    OrganismiThiomicrospira crunogena (strain XCL-2)
    Taxonomic identifieri317025 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira
    ProteomesiUP000002713: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 472472Ribulose bisphosphate carboxylase large chain 1PRO_0000251466Add
    BLAST

    Amino acid modifications

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

    Proteomic databases

    PRIDEiQ31IK0.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi317025.Tcr_0427.

    Structurei

    3D structure databases

    ProteinModelPortaliQ31IK0.
    SMRiQ31IK0. 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.
    OMAiMETWKEV.
    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.

    Q31IK0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKTYNAGVK EYRETYWMPE YEPKDSDFLA CFKVIPQDGV PREEIAAAVA    50
    AESSTGTWTT VWTDLLTDLD YYKGRAYKIE DVPGDDAAFY AFIAYPIDLF 100
    EEGSVVSVMT SLVGNVFGFK ALRACRLEDI RFPLAYVMTC GGPPHGIQVE 150
    RDKMDKYGRP MLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVTS 200
    QPFMRWRDRF LFCQDAIEKA QAETGERKGH YLNCTAGTPE EMYERAEFAK 250
    EIGTPIIMHD YLTGGFTANT GLANYCRKNG LLLHIHRAMH GVIDRNPHHG 300
    IHFRVLTKAL RLSGGDHLHS GTVVGKLEGD REATLGWIDL MRDSFIPEDR 350
    SRGIMFDQDF GAMPGVMPVA SGGIHVWHMP ALVSIFGDDS VLQFGGGTLG 400
    HPWGNAAGAA ANRVALEACV QARNEGKEVE KEGKEILTNA AKHSPELKIA 450
    METWKEIKFE FDTVDKLDVK HK 472
    Length:472
    Mass (Da):52,568
    Last modified:December 6, 2005 - v1
    Checksum:i5E70D6B51D425EC2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000109 Genomic DNA. Translation: ABB41023.1.
    RefSeqiYP_390697.1. NC_007520.2.

    Genome annotation databases

    EnsemblBacteriaiABB41023; ABB41023; Tcr_0427.
    GeneIDi3761246.
    KEGGitcx:Tcr_0427.
    PATRICi23972746. VBIThiCru83387_0439.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000109 Genomic DNA. Translation: ABB41023.1 .
    RefSeqi YP_390697.1. NC_007520.2.

    3D structure databases

    ProteinModelPortali Q31IK0.
    SMRi Q31IK0. Positions 15-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 317025.Tcr_0427.

    Proteomic databases

    PRIDEi Q31IK0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB41023 ; ABB41023 ; Tcr_0427 .
    GeneIDi 3761246.
    KEGGi tcx:Tcr_0427.
    PATRICi 23972746. VBIThiCru83387_0439.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci TCRU317025:GHE8-433-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: XCL-2.

    Entry informationi

    Entry nameiRBL1A_THICR
    AccessioniPrimary (citable) accession number: Q31IK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 60 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