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)

P00880

- RBL_SYNP6

UniProt

P00880 - RBL_SYNP6

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (15 Feb 2005)
      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.

    Kineticsi

    The CO2/O2 specificity factor (tau) is 39.

    1. KM=39 µM for ribulose 1,5-bisphosphate1 Publication
    2. KM=173 µM for CO21 Publication

    Vmax=2.5 µmol/min/mg enzyme with CO2 as substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei120 – 1201Substrate; in homodimeric partner
    Binding sitei170 – 1701Substrate
    Active sitei172 – 1721Proton acceptor
    Binding sitei174 – 1741Substrate
    Metal bindingi198 – 1981Magnesium; via carbamate group
    Metal bindingi200 – 2001Magnesium
    Metal bindingi201 – 2011Magnesium
    Active sitei291 – 2911Proton acceptor
    Binding sitei292 – 2921Substrate
    Binding sitei324 – 3241Substrate
    Sitei331 – 3311Transition state stabilizer
    Binding sitei376 – 3761Substrate

    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

    BioCyciSELO269084:GCDQ-135-MONOMER.
    SABIO-RKP00880.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
    Short name:
    RuBisCO large subunit
    Gene namesi
    Name:cbbL
    Synonyms:rbcA, rbcL
    Ordered Locus Names:syc0130_c
    OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
    Taxonomic identifieri269084 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000001175: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 472472Ribulose bisphosphate carboxylase large chainPRO_0000062651Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei198 – 1981N6-carboxylysine1 Publication

    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. Note this disulfide bond has not been seen in these crystal structures.By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP00880.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-6210N.
    STRINGi269084.syc0130_c.

    Structurei

    Secondary structure

    1
    472
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 214
    Beta strandi32 – 4110
    Helixi47 – 5711
    Turni58 – 603
    Beta strandi63 – 653
    Helixi67 – 715
    Helixi74 – 774
    Beta strandi80 – 867
    Beta strandi94 – 1007
    Helixi102 – 1043
    Helixi110 – 1189
    Helixi121 – 1233
    Beta strandi127 – 13610
    Helixi139 – 1424
    Helixi152 – 1598
    Beta strandi166 – 1683
    Beta strandi172 – 1754
    Helixi179 – 19113
    Beta strandi195 – 1984
    Beta strandi204 – 2063
    Helixi211 – 22919
    Beta strandi234 – 2385
    Helixi244 – 25613
    Beta strandi260 – 2656
    Helixi266 – 2694
    Helixi271 – 28414
    Beta strandi287 – 2915
    Helixi295 – 2995
    Beta strandi302 – 3065
    Helixi308 – 31811
    Beta strandi321 – 3244
    Beta strandi328 – 3325
    Helixi336 – 34712
    Beta strandi349 – 3513
    Helixi355 – 3573
    Beta strandi372 – 3787
    Helixi381 – 3833
    Helixi384 – 3918
    Beta strandi396 – 3983
    Helixi401 – 4044
    Helixi410 – 43021
    Helixi434 – 44815
    Helixi450 – 45910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RBLX-ray2.20A/B/C/D/E/F/G/H6-472[»]
    1RSCX-ray2.30A/B/C/D/E/F/G/H1-472[»]
    2WVWelectron microscopy9.00A/B/C/D/E/F/G/H1-472[»]
    3RG6X-ray3.20A/B1-472[»]
    ProteinModelPortaliP00880.
    SMRiP00880. Positions 6-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00880.

    Family & Domainsi

    Sequence similaritiesi

    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.

    P00880-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA    50
    GAAIAAESST GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY 100
    PLDLFEEGSV TNILTSIVGN VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH 150
    GIQVERDLLN KYGRPMLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD 200
    ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT APTCEEMMKR 250
    AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR 300
    QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH 350
    IEADRSRGVF FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG 400
    GGTLGHPWGN APGATANRVA LEACVQARNE GRDLYREGGD ILREAGKWSP 450
    ELAAALDLWK EIKFEFETMD KL 472
    Length:472
    Mass (Da):52,448
    Last modified:February 15, 2005 - v2
    Checksum:iCDD8519AA9D493C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 392RF → PV(PubMed:6307620)Curated
    Sequence conflicti353 – 3531A → R(PubMed:6307620)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K00486 Genomic DNA. No translation available.
    X03220 Genomic DNA. Translation: CAA26972.1.
    AP008231 Genomic DNA. Translation: BAD78320.1.
    PIRiA90941. RKYCL.
    RefSeqiWP_011242444.1. NC_006576.1.
    YP_170840.1. NC_006576.1.

    Genome annotation databases

    EnsemblBacteriaiBAD78320; BAD78320; syc0130_c.
    GeneIDi3200134.
    KEGGisyc:syc0130_c.
    PATRICi32485757. VBISynElo117686_0157.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K00486 Genomic DNA. No translation available.
    X03220 Genomic DNA. Translation: CAA26972.1 .
    AP008231 Genomic DNA. Translation: BAD78320.1 .
    PIRi A90941. RKYCL.
    RefSeqi WP_011242444.1. NC_006576.1.
    YP_170840.1. NC_006576.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RBL X-ray 2.20 A/B/C/D/E/F/G/H 6-472 [» ]
    1RSC X-ray 2.30 A/B/C/D/E/F/G/H 1-472 [» ]
    2WVW electron microscopy 9.00 A/B/C/D/E/F/G/H 1-472 [» ]
    3RG6 X-ray 3.20 A/B 1-472 [» ]
    ProteinModelPortali P00880.
    SMRi P00880. Positions 6-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6210N.
    STRINGi 269084.syc0130_c.

    Proteomic databases

    PRIDEi P00880.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD78320 ; BAD78320 ; syc0130_c .
    GeneIDi 3200134.
    KEGGi syc:syc0130_c.
    PATRICi 32485757. VBISynElo117686_0157.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SELO269084:GCDQ-135-MONOMER.
    SABIO-RK P00880.

    Miscellaneous databases

    EvolutionaryTracei P00880.

    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 nucleotide sequence for the large subunit of ribulose 1,5-bisphosphate carboxylase from a unicellular cyanobacterium, Synechococcus PCC6301."
      Reichelt B.Y., Delaney S.F.
      DNA 2:121-129(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular cloning and sequence analysis of the cyanobacterial gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase."
      Shinozaki K., Yamada C., Takahata N., Sugiura M.
      Proc. Natl. Acad. Sci. U.S.A. 80:4050-4054(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CARBAMYLATION AT LYS-198.
    3. "Genes for the large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase constitute a single operon in a cyanobacterium Anacystis nidulans 6301."
      Shinozaki K., Sugiura M.
      Mol. Gen. Genet. 200:27-32(1985)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
      Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
      Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
    5. "High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eukaryotic marine algae and properties of recombinant cyanobacterial RubiSCO containing 'algal' residue modifications."
      Read B.A., Tabita F.R.
      Arch. Biochem. Biophys. 312:210-218(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 333-342.
    6. "Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities."
      Horken K.M., Tabita F.R.
      Arch. Biochem. Biophys. 361:183-194(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: KINETIC PARAMETERS.
    7. "The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution."
      Newman J., Gutteridge S.
      J. Biol. Chem. 268:25876-25886(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    8. "Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate."
      Newman J., Gutteridge S.
      Structure 2:495-502(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiRBL_SYNP6
    AccessioniPrimary (citable) accession number: P00880
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 119 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".

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing

    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