Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P54205

- RBL_SYNY3

UniProt

P54205 - RBL_SYNY3

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct
    4. 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

    BioCyciMetaCyc:MONOMER-750.
    SABIO-RKP54205.

    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:slr0009
    OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    Taxonomic identifieri1111708 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    ProteomesiUP000001425: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Ribulose bisphosphate carboxylase large chainPRO_0000062655Add
    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

    PaxDbiP54205.
    PRIDEiP54205.

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    trxAP522313EBI-862277,EBI-862916

    Protein-protein interaction databases

    IntActiP54205. 4 interactions.
    STRINGi1148.slr0009.

    Structurei

    3D structure databases

    ProteinModelPortaliP54205.
    SMRiP54205. Positions 6-464.
    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.
    PhylomeDBiP54205.

    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.

    P54205-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVQAKAGFKA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPAEEAAA    50
    AVAAESSTGT WTTVWTDNLT DLDRYKGRCY DLEAVPNEDN QYFAFIAYPL 100
    DLFEEGSVTN VLTSLVGNVF GFKALRALRL EDIRFPVALI KTFQGPPHGI 150
    TVERDKLNKY GRPLLGCTIK PKLGLSAKNY GRAVYECLRG GLDFTKDDEN 200
    INSQPFMRWR DRFLFVQEAI EKAQAETNEM KGHYLNVTAG TCEEMMKRAE 250
    FAKEIGTPII MHDFFTGGFT ANTTLARWCR DNGILLHIHR AMHAVVDRQK 300
    NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGERGITMGF VDLMREDYVE 350
    EDRSRGIFFT QDYASMPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG 400
    TLGHPWGNAP GATANRVALE ACVQARNEGR NLAREGNDVI REACRWSPEL 450
    AAACELWKEI KFEFEAMDTL 470
    Length:470
    Mass (Da):52,491
    Last modified:October 1, 1996 - v1
    Checksum:i45B9322482745B2B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65960 Genomic DNA. Translation: CAA46773.1.
    BA000022 Genomic DNA. Translation: BAA10190.1.
    PIRiS39561.
    RefSeqiNP_442120.1. NC_000911.1.
    YP_005652178.1. NC_017277.1.
    YP_007451997.1. NC_020286.1.

    Genome annotation databases

    EnsemblBacteriaiBAA10190; BAA10190; BAA10190.
    GeneIDi952593.
    KEGGisyn:slr0009.
    syy:SYNGTS_2225.
    syz:MYO_122490.
    PATRICi23841842. VBISynSp132158_2465.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65960 Genomic DNA. Translation: CAA46773.1 .
    BA000022 Genomic DNA. Translation: BAA10190.1 .
    PIRi S39561.
    RefSeqi NP_442120.1. NC_000911.1.
    YP_005652178.1. NC_017277.1.
    YP_007451997.1. NC_020286.1.

    3D structure databases

    ProteinModelPortali P54205.
    SMRi P54205. Positions 6-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P54205. 4 interactions.
    STRINGi 1148.slr0009.

    Proteomic databases

    PaxDbi P54205.
    PRIDEi P54205.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA10190 ; BAA10190 ; BAA10190 .
    GeneIDi 952593.
    KEGGi syn:slr0009.
    syy:SYNGTS_2225.
    syz:MYO_122490.
    PATRICi 23841842. VBISynSp132158_2465.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi FTQDWAS.
    OrthoDBi EOG6ZKXMS.
    PhylomeDBi P54205.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-750.
    SABIO-RK P54205.

    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. "Construction of a Synechocystis PCC6803 mutant suitable for the study of variant hexadecameric ribulose bisphosphate carboxylase/oxygenase enzymes."
      Amichay D., Levitz R., Gurevitz M.
      Plant Mol. Biol. 23:465-476(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
      Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
      DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27184 / PCC 6803 / N-1.
    3. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
      Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
      , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PCC 6803 / Kazusa.

    Entry informationi

    Entry nameiRBL_SYNY3
    AccessioniPrimary (citable) accession number: P54205
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 105 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
    2. Synechocystis PCC 6803
      Synechocystis (strain PCC 6803): entries and gene names

    External Data

    Dasty 3