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P96486

- RBL_SYNPW

UniProt

P96486 - RBL_SYNPW

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain WH7803)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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 sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
    Binding sitei165 – 1651SubstrateUniRule annotation
    Active sitei167 – 1671Proton acceptorUniRule annotation
    Binding sitei169 – 1691SubstrateUniRule annotation
    Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Active sitei286 – 2861Proton acceptorUniRule annotation
    Binding sitei287 – 2871SubstrateUniRule annotation
    Binding sitei319 – 3191SubstrateUniRule annotation
    Sitei326 – 3261Transition state stabilizerUniRule annotation
    Binding sitei371 – 3711SubstrateUniRule 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:rbcLUniRule annotation
    Ordered Locus Names:SynWH7803_0678
    OrganismiSynechococcus sp. (strain WH7803)
    Taxonomic identifieri32051 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000001566: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 471471Ribulose bisphosphate carboxylase large chainPRO_0000062652Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi32051.SynWH7803_0678.

    Structurei

    3D structure databases

    ProteinModelPortaliP96486.
    SMRiP96486. Positions 15-459.
    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.

    P96486-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKKYDAGVK EYRDTYWTPD YVPLDTDLLA CFKCTGQEGV PKEEVAAAVA    50
    AESSTGTWST VWSELLTDLD FYKGRCYRIE DVPGDKESFY AFIAYPLDLF 100
    EEGSITNVLT SLVGNVFGFK ALRHLRLEDI RFPMAFIKSC YGPPNGIQVE 150
    RDRMNKYGRP LLGCTIKPKL GLSGKNYGRV VYECLRGGLD FTKDDENINS 200
    QPFQRWQNRF EFVAEAIKLS EQETGERKGH YLNVTANTPE EMYERAEFAK 250
    ELGMPIIMHD FITGGFTANT GLSKWCRKNG MLLHIHRAMH AVIDRHPKHG 300
    IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDQ LRESFVPEDR 350
    SRGNFFDQDW GSMPGVFAVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTHG 400
    HPWGSAAGAA ANRVALEACV KARNAGRHLE KESRDILMEA GKHSPELAIA 450
    LETWKEIKFE FDTVDKLDVQ N 471
    Length:471
    Mass (Da):52,848
    Last modified:May 1, 1997 - v1
    Checksum:i96638DF99FD6BF1D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46156 Genomic DNA. Translation: AAB48080.1.
    CT971583 Genomic DNA. Translation: CAK23104.1.
    RefSeqiWP_011932588.1. NC_009481.1.
    YP_001224401.1. NC_009481.1.

    Genome annotation databases

    EnsemblBacteriaiCAK23104; CAK23104; SynWH7803_0678.
    GeneIDi5147701.
    KEGGisyx:SynWH7803_0678.
    PATRICi23827459. VBISynSp43824_0695.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46156 Genomic DNA. Translation: AAB48080.1 .
    CT971583 Genomic DNA. Translation: CAK23104.1 .
    RefSeqi WP_011932588.1. NC_009481.1.
    YP_001224401.1. NC_009481.1.

    3D structure databases

    ProteinModelPortali P96486.
    SMRi P96486. Positions 15-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 32051.SynWH7803_0678.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAK23104 ; CAK23104 ; SynWH7803_0678 .
    GeneIDi 5147701.
    KEGGi syx:SynWH7803_0678.
    PATRICi 23827459. VBISynSp43824_0695.

    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. "Regulation, unique gene organization, and unusual primary structure of carbon fixation genes from a marine phycoerythrin-containing cyanobacterium."
      Watson G.M., Tabita F.R.
      Plant Mol. Biol. 32:1103-1115(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Genoscope
      Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: WH7803.

    Entry informationi

    Entry nameiRBL_SYNPW
    AccessioniPrimary (citable) accession number: P96486
    Secondary accession number(s): A5GJI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 83 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