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P00879

- RBL_NOSS1

UniProt

P00879 - RBL_NOSS1

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (23 Jan 2002)
      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 in the photorespiration process. 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 sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
    Binding sitei174 – 1741SubstrateUniRule annotation
    Active sitei176 – 1761Proton acceptorUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
    Metal bindingi204 – 2041MagnesiumUniRule annotation
    Metal bindingi205 – 2051MagnesiumUniRule annotation
    Active sitei295 – 2951Proton acceptorUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Sitei335 – 3351Transition state stabilizerUniRule annotation
    Binding sitei380 – 3801SubstrateUniRule 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. photorespiration Source: UniProtKB-KW
    2. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    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
    Synonyms:rbc, rbcA, rbcLUniRule annotation
    Ordered Locus Names:alr1524
    OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
    Taxonomic identifieri103690 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
    ProteomesiUP000002483: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 476476Ribulose bisphosphate carboxylase large chainPRO_0000062619Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-carboxylysineUniRule annotation
    Disulfide bondi248 – 248Interchain; 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

    Proteomic databases

    PRIDEiP00879.

    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

    Protein-protein interaction databases

    STRINGi103690.alr1524.

    Structurei

    3D structure databases

    ProteinModelPortaliP00879.
    SMRiP00879. Positions 13-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.
    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.

    P00879-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYAQTKTQT KSGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP    50
    FEEAAAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA 100
    YIAYPLDLFE EGSITNVLTS IVGNVFGFKA LRALRLEDIR FPVAYIKTFQ 150
    GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
    TKDDENINSA PFQRWRDRFL FVADAITKAQ AETGEIKGHY LNVTAPTCEE 250
    MLKRAEYAKE LKQPIIMHDY LTAGFTANTT LARWCRDNGV LLHIHRAMHA 300
    VIDRQKNHGI HFRVLAKALR LSGGDHIHTG TVVGKLEGER GITMGFVDLL 350
    RENYVEQDKS RGIYFTQDWA SLPGVMAVAS GGIHVWHMPA LVEIFGDDSV 400
    LQFGGGTLGH PWGNAPGATA NRVALEACVQ ARNEGRNLAR EGNDVIREAA 450
    KWSPELAVAC ELWKEIKFEF EAMDTV 476
    Length:476
    Mass (Da):53,045
    Last modified:January 23, 2002 - v3
    Checksum:iABEDB246FA2E6A01
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911V → G in AAA22041. (PubMed:16593300)Curated
    Sequence conflicti91 – 911V → G in AAA22024. (PubMed:6091125)Curated
    Sequence conflicti91 – 911V → G in AAA22027. (PubMed:6091125)Curated
    Sequence conflicti91 – 911V → G in AAA22028. (PubMed:6091125)Curated
    Sequence conflicti98 – 981F → S in AAA22041. (PubMed:16593300)Curated
    Sequence conflicti98 – 981F → S in AAA22024. (PubMed:6091125)Curated
    Sequence conflicti98 – 981F → S in AAA22027. (PubMed:6091125)Curated
    Sequence conflicti98 – 981F → S in AAA22028. (PubMed:6091125)Curated
    Sequence conflicti120 – 1201S → Y in AAA22041. (PubMed:16593300)Curated
    Sequence conflicti120 – 1201S → Y in AAA22024. (PubMed:6091125)Curated
    Sequence conflicti120 – 1201S → Y in AAA22027. (PubMed:6091125)Curated
    Sequence conflicti120 – 1201S → Y in AAA22028. (PubMed:6091125)Curated
    Sequence conflicti127 – 1271G → V in AAA22041. (PubMed:16593300)Curated
    Sequence conflicti127 – 1271G → V in AAA22024. (PubMed:6091125)Curated
    Sequence conflicti127 – 1271G → V in AAA22027. (PubMed:6091125)Curated
    Sequence conflicti127 – 1271G → V in AAA22028. (PubMed:6091125)Curated
    Sequence conflicti279 – 2791T → N in AAA22041. (PubMed:16593300)Curated
    Sequence conflicti279 – 2791T → N in AAA22024. (PubMed:6091125)Curated
    Sequence conflicti279 – 2791T → N in AAA22027. (PubMed:6091125)Curated
    Sequence conflicti279 – 2791T → N in AAA22028. (PubMed:6091125)Curated
    Sequence conflicti290 – 2901V → L in AAA22041. (PubMed:16593300)Curated
    Sequence conflicti290 – 2901V → L in AAA22024. (PubMed:6091125)Curated
    Sequence conflicti290 – 2901V → L in AAA22027. (PubMed:6091125)Curated
    Sequence conflicti290 – 2901V → L in AAA22028. (PubMed:6091125)Curated
    Sequence conflicti399 – 3991S → F in AAA22041. (PubMed:16593300)Curated
    Sequence conflicti399 – 3991S → F in AAA22024. (PubMed:6091125)Curated
    Sequence conflicti399 – 3991S → F in AAA22027. (PubMed:6091125)Curated
    Sequence conflicti399 – 3991S → F in AAA22028. (PubMed:6091125)Curated
    Sequence conflicti416 – 4161P → R in AAA22041. (PubMed:16593300)Curated
    Sequence conflicti416 – 4161P → R in AAA22024. (PubMed:6091125)Curated
    Sequence conflicti416 – 4161P → R in AAA22027. (PubMed:6091125)Curated
    Sequence conflicti416 – 4161P → R in AAA22028. (PubMed:6091125)Curated

    Mass spectrometryi

    Molecular mass is 53411 Da from positions 1 - 476. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01540 Genomic DNA. Translation: AAA22041.1.
    L02520 Genomic DNA. Translation: AAA22024.1.
    L02521 Genomic DNA. Translation: AAA22027.1.
    L02522 Genomic DNA. Translation: AAA22028.1.
    BA000019 Genomic DNA. Translation: BAB77890.1.
    PIRiA01099. RKAIL7.
    AF1996.
    RefSeqiNP_485564.1. NC_003272.1.
    WP_010995693.1. NC_003272.1.

    Genome annotation databases

    EnsemblBacteriaiBAB77890; BAB77890; BAB77890.
    GeneIDi1105116.
    KEGGiana:alr1524.
    PATRICi22773054. VBINosSp37423_2010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01540 Genomic DNA. Translation: AAA22041.1 .
    L02520 Genomic DNA. Translation: AAA22024.1 .
    L02521 Genomic DNA. Translation: AAA22027.1 .
    L02522 Genomic DNA. Translation: AAA22028.1 .
    BA000019 Genomic DNA. Translation: BAB77890.1 .
    PIRi A01099. RKAIL7.
    AF1996.
    RefSeqi NP_485564.1. NC_003272.1.
    WP_010995693.1. NC_003272.1.

    3D structure databases

    ProteinModelPortali P00879.
    SMRi P00879. Positions 13-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 103690.alr1524.

    Proteomic databases

    PRIDEi P00879.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB77890 ; BAB77890 ; BAB77890 .
    GeneIDi 1105116.
    KEGGi ana:alr1524.
    PATRICi 22773054. VBINosSp37423_2010.

    Phylogenomic databases

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

    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. "Isolation and sequence of the gene for the large subunit of ribulose-1,5-bisphosphate carboxylase from the cyanobacterium Anabaena 7120."
      Curtis S.E., Haselkorn R.
      Proc. Natl. Acad. Sci. U.S.A. 80:1835-1839(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cotranscription of genes encoding the small and large subunits of ribulose-1,5-bisphosphate carboxylase in the cyanobacterium Anabaena 7120."
      Nierzwicki-Bauer S.A., Curtis S.E., Haselkorn R.
      Proc. Natl. Acad. Sci. U.S.A. 81:5961-5965(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 7120 / UTEX 2576.
    4. Singh H., Rajaram H., Apte S.K.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 16-22, MASS SPECTROMETRY.

    Entry informationi

    Entry nameiRBL_NOSS1
    AccessioniPrimary (citable) accession number: P00879
    Secondary accession number(s): Q60124
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3