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)

P00875

- RBL_SPIOL

UniProt

P00875 - RBL_SPIOL

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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.

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei14 – 141Not N6-methylated
    Binding sitei123 – 1231Substrate; in homodimeric partner
    Binding sitei173 – 1731Substrate
    Active sitei175 – 1751Proton acceptor1 Publication
    Binding sitei177 – 1771Substrate
    Metal bindingi201 – 2011Magnesium; via carbamate group
    Metal bindingi203 – 2031Magnesium
    Metal bindingi204 – 2041Magnesium
    Active sitei294 – 2941Proton acceptor1 Publication
    Binding sitei295 – 2951Substrate
    Binding sitei327 – 3271Substrate
    Sitei334 – 3341Transition state stabilizer
    Binding sitei379 – 3791Substrate

    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
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Protein family/group databases

    Allergomei3814. Spi o RuBisCO.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 221 PublicationPRO_0000031415
    Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_0000031416Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylproline
    Modified residuei201 – 2011N6-carboxylysine1 Publication
    Disulfide bondi247 – 247Interchain; in linked form

    Post-translational modificationi

    The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity. The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.1 Publication

    Protein-protein interaction databases

    DIPiDIP-27641N.
    MINTiMINT-1522611.

    Structurei

    Secondary structure

    1
    475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 244
    Beta strandi36 – 449
    Helixi50 – 5910
    Turni60 – 634
    Beta strandi66 – 683
    Helixi70 – 745
    Helixi77 – 804
    Beta strandi83 – 897
    Beta strandi93 – 953
    Beta strandi97 – 1037
    Helixi105 – 1073
    Helixi113 – 1219
    Helixi124 – 1263
    Beta strandi130 – 13910
    Helixi142 – 1454
    Helixi155 – 1628
    Beta strandi169 – 1713
    Beta strandi175 – 1784
    Helixi182 – 19413
    Beta strandi198 – 2014
    Beta strandi207 – 2093
    Helixi214 – 23219
    Beta strandi237 – 2415
    Helixi247 – 26014
    Beta strandi263 – 2686
    Helixi269 – 2724
    Helixi274 – 28714
    Beta strandi290 – 2945
    Helixi298 – 3025
    Beta strandi305 – 3095
    Helixi311 – 32111
    Beta strandi324 – 3274
    Beta strandi331 – 3355
    Helixi339 – 35012
    Beta strandi352 – 3543
    Helixi358 – 3603
    Beta strandi375 – 3817
    Helixi384 – 3863
    Helixi387 – 3948
    Beta strandi396 – 4016
    Helixi404 – 4074
    Helixi413 – 43220
    Helixi437 – 44812
    Turni449 – 4513
    Helixi453 – 46210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AA1X-ray2.20B/E/H/L1-475[»]
    1AUSX-ray2.20L/M/N/O1-475[»]
    1IR1X-ray1.80A/B/C/D1-475[»]
    1RBOX-ray2.30B/E/H/L1-475[»]
    1RCOX-ray2.30B/E/H/K/L/O/R/V1-475[»]
    1RCXX-ray2.40B/E/H/K/L/O/R/V1-475[»]
    1RXOX-ray2.20B/E/H/L1-475[»]
    1UPMX-ray2.30B/E/H/K/L/O/R/V1-475[»]
    1UPPX-ray2.30A/C/E/G1-475[»]
    8RUCX-ray1.60A/C/E/G1-475[»]
    ProteinModelPortaliP00875.
    SMRiP00875. Positions 9-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00875.

    Family & Domainsi

    Sequence similaritiesi

    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.

    P00875-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPQTETKAS VEFKAGVKDY KLTYYTPEYE TLDTDILAAF RVSPQPGVPP    50
    EEAGAAVAAE SSTGTWTTVW TDGLTNLDRY KGRCYHIEPV AGEENQYICY 100
    VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PVAYVKTFQG 150
    PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
    KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL NATAGTCEDM 250
    MKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV 300
    IDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERD ITLGFVDLLR 350
    DDYTEKDRSR GIYFTQSWVS TPGVLPVASG GIHVWHMPAL TEIFGDDSVL 400
    QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNTIIREATK 450
    WSPELAAACE VWKEIKFEFP AMDTV 475
    Length:475
    Mass (Da):52,740
    Last modified:July 21, 1986 - v1
    Checksum:i484FFFFD36BB1238
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121E → G in CAB88737. (PubMed:11292076)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00168 Genomic DNA. Translation: CAA23473.1.
    AJ400848 Genomic DNA. Translation: CAB88737.1.
    PIRiA01094. RKSPL.
    A28965.
    RefSeqiNP_054944.1. NC_002202.1.

    Genome annotation databases

    GeneIDi2715621.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The Plant Kingdom's sloth - Issue 38 of September 2003

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00168 Genomic DNA. Translation: CAA23473.1 .
    AJ400848 Genomic DNA. Translation: CAB88737.1 .
    PIRi A01094. RKSPL.
    A28965.
    RefSeqi NP_054944.1. NC_002202.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AA1 X-ray 2.20 B/E/H/L 1-475 [» ]
    1AUS X-ray 2.20 L/M/N/O 1-475 [» ]
    1IR1 X-ray 1.80 A/B/C/D 1-475 [» ]
    1RBO X-ray 2.30 B/E/H/L 1-475 [» ]
    1RCO X-ray 2.30 B/E/H/K/L/O/R/V 1-475 [» ]
    1RCX X-ray 2.40 B/E/H/K/L/O/R/V 1-475 [» ]
    1RXO X-ray 2.20 B/E/H/L 1-475 [» ]
    1UPM X-ray 2.30 B/E/H/K/L/O/R/V 1-475 [» ]
    1UPP X-ray 2.30 A/C/E/G 1-475 [» ]
    8RUC X-ray 1.60 A/C/E/G 1-475 [» ]
    ProteinModelPortali P00875.
    SMRi P00875. Positions 9-475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-27641N.
    MINTi MINT-1522611.

    Protein family/group databases

    Allergomei 3814. Spi o RuBisCO.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2715621.

    Miscellaneous databases

    EvolutionaryTracei P00875.

    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. "The structure of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from spinach chloroplast DNA."
      Zurawski G., Perrot B., Bottomley W., Whitfeld P.R.
      Nucleic Acids Res. 9:3251-3270(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide sequence and gene organization."
      Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G., Mache R.
      Plant Mol. Biol. 45:307-315(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Geant d'hiver and cv. Monatol.
    3. "Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase."
      Houtz R.L., Stults J.T., Mulligan R.M., Tolbert N.E.
      Proc. Natl. Acad. Sci. U.S.A. 86:1855-1859(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 3-18, LACK OF METHYLATION.
    4. "Reaction-intermediate analogue binding by ribulose bisphosphate carboxylase/oxygenase causes specific changes in proteolytic sensitivity: the amino-terminal residue of the large subunit is acetylated proline."
      Mulligan R.M., Houtz R.L., Tolbert N.E.
      Proc. Natl. Acad. Sci. U.S.A. 85:1513-1517(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 8-14 AND 466-475.
    5. "Sequences of two active-site peptides from spinach ribulosebisphosphate carboxylase/oxygenase."
      Stringer C.D., Hartman F.C.
      Biochem. Biophys. Res. Commun. 80:1043-1048(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    6. Lorimer G.H.
      Submitted (OCT-1982) to the PIR data bank
      Cited for: ACTIVATION.
    7. "Reexamination of the three-dimensional structure of the small subunit of RuBisCo from higher plants."
      Knight S., Andersson I., Braenden C.-I.
      Science 244:702-705(1989)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    8. "Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4-A resolution. Subunit interactions and active site."
      Knight S., Andersson I., Braenden C.-I.
      J. Mol. Biol. 215:113-160(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    9. "Large structures at high resolution: the 1.6-A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate."
      Andersson I.
      J. Mol. Biol. 259:160-174(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    10. "A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate."
      Taylor T.C., Fothergill M.D., Andersson I.
      J. Biol. Chem. 271:32894-32899(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH INHIBITORS 4-CABP AND XUBP.
    11. "Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase."
      Taylor T.C., Andersson I.
      Biochemistry 36:4041-4046(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), CARBAMYLATION AT LYS-201.
    12. "The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate."
      Taylor T.C., Andersson I.
      J. Mol. Biol. 265:432-444(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    13. "Calcium supports loop closure but not catalysis in Rubisco."
      Karkehabadi S., Taylor T.C., Andersson I.
      J. Mol. Biol. 334:65-73(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiRBL_SPIOL
    AccessioniPrimary (citable) accession number: P00875
    Secondary accession number(s): Q9M3L8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 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".

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3