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P0C2C2

- RBL1C_CUPNE

UniProt

P0C2C2 - RBL1C_CUPNE

Protein

Ribulose bisphosphate carboxylase large chain, chromosomal

Gene

cbbL1

Organism
Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      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.

    Catalytic activityi

    2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

    Cofactori

    Binds 1 magnesium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei126 – 1261Substrate; in homodimeric partner
    Binding sitei176 – 1761Substrate
    Active sitei178 – 1781Proton acceptor
    Binding sitei180 – 1801Substrate
    Metal bindingi204 – 2041Magnesium; via carbamate group
    Metal bindingi206 – 2061Magnesium
    Metal bindingi207 – 2071Magnesium
    Active sitei296 – 2961Proton acceptor
    Binding sitei297 – 2971Substrate
    Binding sitei329 – 3291Substrate
    Sitei336 – 3361Transition state stabilizer
    Binding sitei381 – 3811Substrate

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain, chromosomal (EC:4.1.1.39)
    Short name:
    RuBisCO large subunit
    Gene namesi
    Name:cbbL1
    Synonyms:cbbL, cbxLC, cfxLC
    OrganismiCupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
    Taxonomic identifieri106590 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Ribulose bisphosphate carboxylase large chain, chromosomalPRO_0000062641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei204 – 2041N6-carboxylysine1 Publication

    Post-translational modificationi

    The disulfide bond which can form between Cys-278 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni25 – 273
    Beta strandi38 – 4710
    Helixi53 – 6210
    Turni63 – 664
    Helixi75 – 784
    Helixi81 – 833
    Beta strandi86 – 927
    Beta strandi100 – 1078
    Helixi108 – 1103
    Helixi116 – 1249
    Helixi127 – 1293
    Beta strandi133 – 1353
    Beta strandi137 – 1426
    Helixi145 – 1484
    Helixi158 – 1658
    Beta strandi172 – 1765
    Helixi185 – 19713
    Beta strandi201 – 2044
    Helixi217 – 23519
    Beta strandi240 – 2445
    Helixi250 – 26213
    Beta strandi266 – 2716
    Helixi272 – 2743
    Helixi276 – 28712
    Turni288 – 2903
    Beta strandi292 – 2965
    Turni298 – 3003
    Helixi301 – 3044
    Beta strandi309 – 3113
    Helixi313 – 32311
    Beta strandi326 – 3294
    Beta strandi335 – 3384
    Helixi341 – 35212
    Beta strandi354 – 3563
    Helixi360 – 3623
    Beta strandi377 – 3837
    Helixi386 – 3883
    Helixi389 – 3968
    Beta strandi401 – 4044
    Helixi406 – 4094
    Helixi414 – 43522
    Helixi439 – 45315
    Helixi455 – 4639

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BXNX-ray2.70A/C/E/G1-486[»]
    ProteinModelPortaliP0C2C2.
    SMRiP0C2C2. Positions 24-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C2C2.

    Family & Domainsi

    Sequence similaritiesi

    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.

    P0C2C2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAPETIQAK PRKRYDAGVM KYKEMGYWDG DYVPKDTDVL ALFRITPQDG    50
    VDPVEAAAAV AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF 100
    FCYVAYDLSL FEEGSIANLT ASIIGNVFSF KPIKAARLED MRFPVAYVKT 150
    FAGPSTGIIV ERERLDKFGR PLLGATTKPK LGLSGRNYGR VVYEGLKGGL 200
    DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG SYLNVTAGTM 250
    EEMYRRAEFA KSLGSVIIMV DLIVGWTCIQ SMSNWCRQND MILHLHRAGH 300
    GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV 350
    CRDAYTQTDL TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV 400
    VLQFGGGTIG HPQGIQAGAT ANRVALEAMV LARNEGRDIL NEGPEILRDA 450
    ARWCAPLRAA LDTWGDITFN YTPTDTSDFV PTASVA 486
    Length:486
    Mass (Da):53,840
    Last modified:January 23, 2007 - v1
    Checksum:i66EAB4A11982FAB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17744 Genomic DNA. Translation: AAC28129.1.
    PIRiA26954. RKALLE.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17744 Genomic DNA. Translation: AAC28129.1 .
    PIRi A26954. RKALLE.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BXN X-ray 2.70 A/C/E/G 1-486 [» ]
    ProteinModelPortali P0C2C2.
    SMRi P0C2C2. Positions 24-467.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P0C2C2.

    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. "Sequence analysis of the Alcaligenes eutrophus chromosomally encoded ribulose bisphosphate carboxylase large and small subunit genes and their gene products."
      Andersen K., Caton J.
      J. Bacteriol. 169:4547-4558(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CARBAMYLATION AT LYS-204.
      Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.
    2. Andersen K.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits."
      Hansen S., Vollan V.B., Hough E., Andersen K.
      J. Mol. Biol. 288:609-621(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
      Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.

    Entry informationi

    Entry nameiRBL1C_CUPNE
    AccessioniPrimary (citable) accession number: P0C2C2
    Secondary accession number(s): P09657, P77811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 41 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".

    Keywords - Technical termi

    3D-structure

    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