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P27066

- RBL_SOYBN

UniProt

P27066 - RBL_SOYBN

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 3 (21 Feb 2006)
      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.

    Catalytic activityi

    2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei123 – 1231Substrate; in homodimeric partnerBy similarity
    Binding sitei173 – 1731SubstrateBy similarity
    Active sitei175 – 1751Proton acceptorBy similarity
    Binding sitei177 – 1771SubstrateBy similarity
    Metal bindingi201 – 2011Magnesium; via carbamate groupBy similarity
    Metal bindingi203 – 2031MagnesiumBy similarity
    Metal bindingi204 – 2041MagnesiumBy similarity
    Active sitei294 – 2941Proton acceptorBy similarity
    Binding sitei295 – 2951SubstrateBy similarity
    Binding sitei327 – 3271SubstrateBy similarity
    Sitei334 – 3341Transition state stabilizerBy similarity
    Binding sitei379 – 3791SubstrateBy similarity

    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 chain (EC:4.1.1.39)
    Short name:
    RuBisCO large subunit
    Gene namesi
    Name:rbcL
    Encoded oniPlastid; Chloroplast
    OrganismiGlycine max (Soybean) (Glycine hispida)
    Taxonomic identifieri3847 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
    ProteomesiUP000008827: Chloroplast

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 221 PublicationPRO_0000031411
    Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_0000031412Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylproline1 Publication
    Modified residuei14 – 141N6,N6,N6-trimethyllysine1 Publication
    Modified residuei201 – 2011N6-carboxylysineBy similarity
    Disulfide bondi247 – 247Interchain; in linked formBy similarity

    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.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Methylation

    Expressioni

    Gene expression databases

    GenevestigatoriP27066.

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP27066.
    SMRiP27066. Positions 9-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    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.

    P27066-1 [UniParc]FASTAAdd to Basket

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    MSPQTETKAS VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVTPQPGVPP    50
    EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYGLEPV AGEENQYIAY 100
    VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PTAYIKTFQG 150
    PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
    KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL NATAGTCEEM 250
    MKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 300
    IDRQKNHGMH FRVLAKALRL SGGDHVHAGT VVGKLEGERE ITLGFVDLLR 350
    DDFVEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL 400
    QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK 450
    WSPELAAACE VWKEIKFEFE AMDTL 475
    Length:475
    Mass (Da):52,610
    Last modified:February 21, 2006 - v3
    Checksum:i481460745D587783
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431A → S in CAB08877. (PubMed:9242596)Curated
    Sequence conflicti470 – 4701E → P in CAB08877. (PubMed:9242596)Curated
    Sequence conflicti474 – 4752Missing in CAB08877. (PubMed:9242596)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z95552 Genomic DNA. Translation: CAB08877.1.
    DQ317523 Genomic DNA. Translation: ABC25107.1.
    RefSeqiYP_538747.1. NC_007942.1.

    Genome annotation databases

    GeneIDi3989271.
    KEGGigmx:3989271.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z95552 Genomic DNA. Translation: CAB08877.1 .
    DQ317523 Genomic DNA. Translation: ABC25107.1 .
    RefSeqi YP_538747.1. NC_007942.1.

    3D structure databases

    ProteinModelPortali P27066.
    SMRi P27066. Positions 9-463.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3989271.
    KEGGi gmx:3989271.

    Phylogenomic databases

    KOi K01601.

    Gene expression databases

    Genevestigatori P27066.

    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. "Phylogenetic relationships in the Papilionoideae (family Leguminosae) based on nucleotide sequences of cpDNA (rbcL) and ncDNA (ITS 1 and 2)."
      Kaess E., Wink M.
      Mol. Phylogenet. Evol. 8:65-88(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leaf.
    2. "Complete chloroplast genome sequence of Glycine max and comparative analyses with other legume genomes."
      Saski C., Lee S.-B., Daniell H., Wood T.C., Tomkins J., Kim H.-G., Jansen R.K.
      Plant Mol. Biol. 59:309-322(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. PI 437654.
    3. "Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species."
      Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.
      Plant Physiol. 98:1170-1174(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14, ACETYLATION AT PRO-3.

    Entry informationi

    Entry nameiRBL_SOYBN
    AccessioniPrimary (citable) accession number: P27066
    Secondary accession number(s): Q2PMV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: February 21, 2006
    Last modified: October 1, 2014
    This is version 91 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant 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" By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3