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O85040

- RBL1_HALNC

UniProt

O85040 - RBL1_HALNC

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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

    BioCyciHNEA555778:GIVV-951-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:Hneap_0922
    OrganismiHalothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
    Taxonomic identifieri555778 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesHalothiobacillaceaeHalothiobacillus
    ProteomesiUP000009102: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473Ribulose bisphosphate carboxylase large chainPRO_0000062660Add
    BLAST

    Amino acid modifications

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

    Expressioni

    Inductioni

    Produced when grown in air or in air supplemented with 5% CO2.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi555778.Hneap_0922.

    Structurei

    Secondary structure

    1
    473
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 3710
    Helixi43 – 5311
    Turni54 – 563
    Helixi63 – 675
    Turni70 – 723
    Beta strandi76 – 838
    Beta strandi86 – 9611
    Helixi98 – 1003
    Helixi106 – 1149
    Helixi117 – 1193
    Beta strandi123 – 13210
    Helixi135 – 1384
    Helixi148 – 1558
    Beta strandi162 – 1665
    Beta strandi170 – 1723
    Helixi175 – 18713
    Beta strandi191 – 1944
    Beta strandi200 – 2023
    Helixi207 – 22519
    Beta strandi230 – 2345
    Helixi240 – 25314
    Beta strandi257 – 2615
    Turni262 – 2654
    Helixi267 – 28014
    Beta strandi283 – 2875
    Helixi291 – 2955
    Beta strandi300 – 3023
    Helixi304 – 31411
    Beta strandi317 – 3204
    Helixi329 – 3313
    Helixi333 – 34311
    Beta strandi345 – 3473
    Helixi351 – 3533
    Beta strandi368 – 3747
    Helixi377 – 3793
    Helixi380 – 3878
    Beta strandi389 – 3946
    Helixi397 – 4004
    Helixi406 – 42520
    Turni430 – 4334
    Helixi434 – 4429
    Helixi446 – 45510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SVDX-ray1.80A1-473[»]
    ProteinModelPortaliO85040.
    SMRiO85040. Positions 16-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO85040.

    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.

    O85040-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVKKYSAGV KEYRQTYWMP EYTPLDSDIL ACFKITPQPG VDREEAAAAV    50
    AAESSTGTWT TVWTDLLTDM DYYKGRAYRI EDVPGDDAAF YAFIAYPIDL 100
    FEEGSVVNVF TSLVGNVFGF KAVRGLRLED VRFPLAYVKT CGGPPHGIQV 150
    ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENIN 200
    SQPFMRWRDR FLFVQDATET AEAQTGERKG HYLNVTAPTP EEMYKRAEFA 250
    KEIGAPIIMH DYITGGFTAN TGLAKWCQDN GVLLHIHRAM HAVIDRNPNH 300
    GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFIPED 350
    RSRGIFFDQD WGSMPGVFAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL 400
    GHPWGNAAGA AANRVALEAC VEARNQGRDI EKEGKEILTA AAQHSPELKI 450
    AMETWKEIKF EFDTVDKLDT QNR 473
    Length:473
    Mass (Da):52,636
    Last modified:November 1, 1998 - v1
    Checksum:iB84D2EDE46CAF7D8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038430 Genomic DNA. Translation: AAC32549.1.
    CP001801 Genomic DNA. Translation: ACX95765.1.
    RefSeqiWP_012823801.1. NC_013422.1.
    YP_003262812.1. NC_013422.1.

    Genome annotation databases

    EnsemblBacteriaiACX95765; ACX95765; Hneap_0922.
    GeneIDi8534063.
    KEGGihna:Hneap_0922.
    PATRICi32205718. VBIHalNea120669_0941.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038430 Genomic DNA. Translation: AAC32549.1 .
    CP001801 Genomic DNA. Translation: ACX95765.1 .
    RefSeqi WP_012823801.1. NC_013422.1.
    YP_003262812.1. NC_013422.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SVD X-ray 1.80 A 1-473 [» ]
    ProteinModelPortali O85040.
    SMRi O85040. Positions 16-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 555778.Hneap_0922.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACX95765 ; ACX95765 ; Hneap_0922 .
    GeneIDi 8534063.
    KEGGi hna:Hneap_0922.
    PATRICi 32205718. VBIHalNea120669_0941.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci HNEA555778:GIVV-951-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O85040.

    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. "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth."
      Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.
      J. Bacteriol. 180:4133-4139(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 23641 / c2.
    3. "The structure of Halothiobacillus neapolitanus Rubisco."
      Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E., Tran K., Yeates T.O.
      Submitted (APR-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiRBL1_HALNC
    AccessioniPrimary (citable) accession number: O85040
    Secondary accession number(s): D0KZ92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 77 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3