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P22859

- RBL1B_ALLVD

UniProt

P22859 - RBL1B_ALLVD

Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 4 (15 Jun 2010)
      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.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, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciAVIN572477:GCJK-2812-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
    Synonyms:rbcLUniRule annotation
    Ordered Locus Names:Alvin_2750
    OrganismiAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum)
    Taxonomic identifieri572477 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium
    ProteomesiUP000001441: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 471470Ribulose bisphosphate carboxylase large chain 2PRO_0000062622Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-carboxylysineUniRule annotation
    Disulfide bondi240 – 240Interchain; in linked formUniRule annotation

    Post-translational modificationi

    The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

    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.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP22859.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000230831.
    KOiK01601.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22859-1 [UniParc]FASTAAdd to Basket

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    MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV    50
    AAESSTGTWT TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL 100
    FEEGSIVNVL TSLVGNVFGF KAVRALRLED IRFPLHYVKT CGGPPNGIQV 150
    ERDRMDKYGR PFLGATVKPK LGLSAKNYGR AVYEMLRGGL DFTKDDENVN 200
    SQPFMRWQNR FEFVSEAVRK AQEETGERKG HYLNVTAPTC EEMFKRAEFA 250
    KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRNPKH 300
    GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED 350
    RSRGLFFDQD WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ 400
    GHPWGNAAGA AANRVATEAC VKARNEGVEI EKHAREVLSD AARHSPELAV 450
    AMETWKEIKF EFDVVDKLDA A 471
    Length:471
    Mass (Da):52,284
    Last modified:June 15, 2010 - v4
    Checksum:i08A26940B6458D97
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451P → R in BAA14229. (PubMed:1899846)Curated
    Sequence conflicti222 – 2221Q → R in BAA14229. (PubMed:1899846)Curated
    Sequence conflicti297 – 2971N → H in BAA14229. (PubMed:1899846)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90204 Genomic DNA. Translation: BAA14229.1.
    CP001896 Genomic DNA. Translation: ADC63659.1.
    PIRiJQ0586. RKKRL2.
    RefSeqiYP_003444691.1. NC_013851.1.

    Genome annotation databases

    EnsemblBacteriaiADC63659; ADC63659; Alvin_2750.
    GeneIDi8788139.
    KEGGialv:Alvin_2750.
    PATRICi31925280. VBIAllVin64954_2712.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90204 Genomic DNA. Translation: BAA14229.1 .
    CP001896 Genomic DNA. Translation: ADC63659.1 .
    PIRi JQ0586. RKKRL2.
    RefSeqi YP_003444691.1. NC_013851.1.

    3D structure databases

    ProteinModelPortali P22859.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADC63659 ; ADC63659 ; Alvin_2750 .
    GeneIDi 8788139.
    KEGGi alv:Alvin_2750.
    PATRICi 31925280. VBIAllVin64954_2712.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.

    Enzyme and pathway databases

    BioCyci AVIN572477:GCJK-2812-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. "Sequence and expression of genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum."
      Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K., Shinozaki K., Kobayashi K., Sugiura M.
      Gene 97:55-62(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete sequence of chromosome of Allochromatium vinosum DSM 180."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T.
      Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D.
    3. "Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum."
      Viale A.M., Kobayashi H., Akazawa T.
      J. Biol. Chem. 265:18386-18392(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-26.

    Entry informationi

    Entry nameiRBL1B_ALLVD
    AccessioniPrimary (citable) accession number: P22859
    Secondary accession number(s): D3RQ48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 93 of the entry and version 4 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

    Caution

    In C.vinosum two similar set of genes code for RuBisCO large and small chains: the RbcL-RbcS and the RbcA-RbcB sets. Under standard photoautotrophic culture conditions only the latter set seems active, the former probably being cryptic.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3