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Q44176

- RBL_SYNP2

UniProt

Q44176 - RBL_SYNP2

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (01 Jul 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 sitei118 – 1181Substrate; in homodimeric partnerUniRule annotation
    Binding sitei168 – 1681SubstrateUniRule annotation
    Active sitei170 – 1701Proton acceptorUniRule annotation
    Binding sitei172 – 1721SubstrateUniRule annotation
    Metal bindingi196 – 1961Magnesium; via carbamate groupUniRule annotation
    Metal bindingi198 – 1981MagnesiumUniRule annotation
    Metal bindingi199 – 1991MagnesiumUniRule annotation
    Active sitei289 – 2891Proton acceptorUniRule annotation
    Binding sitei290 – 2901SubstrateUniRule annotation
    Binding sitei322 – 3221SubstrateUniRule annotation
    Sitei329 – 3291Transition state stabilizerUniRule annotation
    Binding sitei374 – 3741SubstrateUniRule 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

    Enzyme and pathway databases

    BioCyciSSP32049:GKF7-1799-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
    Synonyms:rbcLUniRule annotation
    Ordered Locus Names:SYNPCC7002_A1798
    OrganismiSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
    Taxonomic identifieri32049 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000001688: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Ribulose bisphosphate carboxylase large chainPRO_0000062650Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei196 – 1961N6-carboxylysineUniRule annotation
    Disulfide bondi242 – 242Interchain; 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

    PRIDEiQ44176.

    PTM databases

    PhosSiteiP13051899.

    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

    STRINGi32049.SYNPCC7002_A1798.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PEMX-ray2.95R459-465[»]
    ProteinModelPortaliQ44176.
    SMRiQ44176. Positions 5-470.
    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.

    Q44176-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQTKSAGFNA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPPEECAA    50
    AVAAESSTGT WTTVWTDGLT DLDRYKGRCY NVEPVPGEDN QYFCFVAYPL 100
    DLFEEGSVTN VLTSLVGNVF GFKALRALRL EDIRFPVALI KTYQGPPHGI 150
    TVERDLLNKY GRPLLGCTIK PKLGLSAKNY GRAVYECLRG GLDFTKDDEN 200
    INSQPFMRWR DRFLFVQEAI EKSQAETNEV KGHYLNVTAG TCEEMLKRAE 250
    FAKEIGTPII MHDFLTGGFT ANTTLAKWCR DNGVLLHIHR AMHAVIDRQK 300
    NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGDRAATLGF VDLMREDYVE 350
    EDRSRGVFFT QDYASLPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG 400
    TLGHPWGNAP GATANRVALE ACVQARNEGR SLAREGNDVL REAGKWSPEL 450
    AAALDLWKEI KFEFDTVDTL 470
    Length:470
    Mass (Da):52,159
    Last modified:July 1, 1997 - v2
    Checksum:i7D43456FD17D9775
    GO

    Sequence cautioni

    The sequence ACA99786.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13971 Genomic DNA. Translation: BAA03076.1.
    CP000951 Genomic DNA. Translation: ACA99786.1. Different initiation.
    RefSeqiWP_012307409.1. NC_010475.1.
    YP_001735042.1. NC_010475.1.

    Genome annotation databases

    EnsemblBacteriaiACA99786; ACA99786; SYNPCC7002_A1798.
    GeneIDi6056494.
    KEGGisyp:SYNPCC7002_A1798.
    PATRICi23818226. VBISynSp37135_2054.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13971 Genomic DNA. Translation: BAA03076.1 .
    CP000951 Genomic DNA. Translation: ACA99786.1 . Different initiation.
    RefSeqi WP_012307409.1. NC_010475.1.
    YP_001735042.1. NC_010475.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PEM X-ray 2.95 R 459-465 [» ]
    ProteinModelPortali Q44176.
    SMRi Q44176. Positions 5-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 32049.SYNPCC7002_A1798.

    PTM databases

    PhosSitei P13051899.

    Proteomic databases

    PRIDEi Q44176.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACA99786 ; ACA99786 ; SYNPCC7002_A1798 .
    GeneIDi 6056494.
    KEGGi syp:SYNPCC7002_A1798.
    PATRICi 23818226. VBISynSp37135_2054.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SSP32049:GKF7-1799-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. "Cloning and characterization of RubisCO large subunit and small subunit from Synechococcus sp. PCC7002."
      Akiyama H., Kanai S., Hirano M., Sugimoto M., Kiyohara M.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete sequence of Synechococcus sp. PCC 7002."
      Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
      Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27264 / PCC 7002 / PR-6.

    Entry informationi

    Entry nameiRBL_SYNP2
    AccessioniPrimary (citable) accession number: Q44176
    Secondary accession number(s): B1XPS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 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