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Q31HD9

- RBL1B_THICR

UniProt

Q31HD9 - RBL1B_THICR

Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

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 sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
    Binding sitei166 – 1661SubstrateUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei170 – 1701SubstrateUniRule annotation
    Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Metal bindingi197 – 1971MagnesiumUniRule annotation
    Active sitei287 – 2871Proton acceptorUniRule annotation
    Binding sitei288 – 2881SubstrateUniRule annotation
    Binding sitei320 – 3201SubstrateUniRule annotation
    Sitei327 – 3271Transition state stabilizerUniRule annotation
    Binding sitei372 – 3721SubstrateUniRule 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:GHE8-857-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain 2UniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunit 2UniRule annotation
    Gene namesi
    Name:cbbL2UniRule annotation
    Ordered Locus Names:Tcr_0838
    OrganismiThiomicrospira crunogena (strain XCL-2)
    Taxonomic identifieri317025 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira
    ProteomesiUP000002713: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 471471Ribulose bisphosphate carboxylase large chain 2PRO_0000251467Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-carboxylysineUniRule annotation

    Proteomic databases

    PRIDEiQ31HD9.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi317025.Tcr_0838.

    Structurei

    3D structure databases

    ProteinModelPortaliQ31HD9.
    SMRiQ31HD9. Positions 16-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiIGNDIST.
    OrthoDBiEOG6ZKXMS.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01338. RuBisCO_L_type1.
    InterProiIPR020888. 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.

    Sequencei

    Sequence statusi: Complete.

    Q31HD9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASKTFDAGV QDYQLTYWTP DYTPLDTDLL ACFKVVPQDG VPREEAAAAV    50
    AAESSTGTWT TVWTDLLTDM EFYKGRCYRI EDVPGDKNAF YAFIAYPLDL 100
    FEEGSVVNVL TSLVGNVFGF KAVRSLRLED LRFPIAFIKT CGGPPAGIQV 150
    ERDKLNKYGR PMLGCTIKPK LGLSAKNYGR AVYECLRGGL DLTKDDENIN 200
    SQPFQRWQNR FEFVADAVDK ATAETGERKG HYLNVTAGTV EEMMKRAEFA 250
    KELGQPIIMH DFLTAGFTAN TTLANWCRDN GMLLHIHRAM HAVIDRNPNH 300
    GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRASTLGFVD QLREAFVPED 350
    RSRGVFFDQD WGSMPGVMAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTQ 400
    GHPGGNAAGA AANRVALEAC VKARNEGRDL EREGGDILRD AARNSKELAV 450
    ALDTWKEIKF EFDTVDKLDV G 471
    Length:471
    Mass (Da):51,865
    Last modified:December 6, 2005 - v1
    Checksum:i3568693BCFA7BBDD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000109 Genomic DNA. Translation: ABB41434.1.
    RefSeqiYP_391108.1. NC_007520.2.

    Genome annotation databases

    EnsemblBacteriaiABB41434; ABB41434; Tcr_0838.
    GeneIDi3760532.
    KEGGitcx:Tcr_0838.
    PATRICi23973632. VBIThiCru83387_0873.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000109 Genomic DNA. Translation: ABB41434.1 .
    RefSeqi YP_391108.1. NC_007520.2.

    3D structure databases

    ProteinModelPortali Q31HD9.
    SMRi Q31HD9. Positions 16-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 317025.Tcr_0838.

    Proteomic databases

    PRIDEi Q31HD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB41434 ; ABB41434 ; Tcr_0838 .
    GeneIDi 3760532.
    KEGGi tcx:Tcr_0838.
    PATRICi 23973632. VBIThiCru83387_0873.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci TCRU317025:GHE8-857-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 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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: XCL-2.

    Entry informationi

    Entry nameiRBL1B_THICR
    AccessioniPrimary (citable) accession number: Q31HD9
    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