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P00874

- RBL_MAIZE

UniProt

P00874 - RBL_MAIZE

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      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 sitei123 – 1231Substrate; in homodimeric partnerUniRule annotation
    Binding sitei173 – 1731SubstrateUniRule annotation
    Active sitei175 – 1751Proton acceptorUniRule annotation
    Binding sitei177 – 1771SubstrateUniRule annotation
    Metal bindingi201 – 2011Magnesium; via carbamate groupUniRule annotation
    Metal bindingi203 – 2031MagnesiumUniRule annotation
    Metal bindingi204 – 2041MagnesiumUniRule annotation
    Active sitei294 – 2941Proton acceptorUniRule annotation
    Binding sitei295 – 2951SubstrateUniRule annotation
    Binding sitei327 – 3271SubstrateUniRule annotation
    Sitei334 – 3341Transition state stabilizerUniRule annotation
    Binding sitei379 – 3791SubstrateUniRule 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

    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:rbcLUniRule annotation
    Encoded oniPlastid; Chloroplast
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
    ProteomesiUP000007305: Chloroplast

    Organism-specific databases

    GrameneiP00874.
    MaizeGDBi69185.

    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 – 22UniRule annotationPRO_0000031295
    Chaini3 – 476474Ribulose bisphosphate carboxylase large chainPRO_0000031296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylprolineUniRule annotation
    Modified residuei14 – 141N6,N6,N6-trimethyllysineUniRule annotation
    Modified residuei201 – 2011N6-carboxylysineUniRule annotation
    Disulfide bondi247 – 247Interchain; 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

    Acetylation, Disulfide bond, Methylation

    Proteomic databases

    PRIDEiP00874.

    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

    Structurei

    3D structure databases

    ProteinModelPortaliP00874.
    SMRiP00874. Positions 11-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000230831.
    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.

    P00874-1 [UniParc]FASTAAdd to Basket

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    MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQLGVPP    50
    EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGDPDQYICY 100
    VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFQG 150
    PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRACY ECLRGGLDFT 200
    KDDENVNSQP FMRWRDRFVF CAEAIYKAQA ETGEIKGHYL NATAGTCEEM 250
    IKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV 300
    IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE ITLGFVDLLR 350
    DDFIEKDRSR GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL 400
    QFGGGTLGHP WGNAPGAAAN RVALEACVQA RNEGRDLARE GNEIIKAACK 450
    WSAELAAACE IWKEIKFDGF KAMDTI 476
    Length:476
    Mass (Da):52,701
    Last modified:November 1, 1995 - v2
    Checksum:i07ECB650E0C8F6E3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631T → AA in CAA23474. 1 PublicationCurated
    Sequence conflicti153 – 1531H → R1 PublicationCurated
    Sequence conflicti155 – 1551I → M1 PublicationCurated
    Sequence conflicti228 – 2281A → S in CAA23474. 1 PublicationCurated
    Sequence conflicti248 – 2481E → D in CAA23474. 1 PublicationCurated
    Sequence conflicti253 – 2531R → G in CAA23474. 1 PublicationCurated
    Sequence conflicti259 – 2591E → Q in CAA23474. 1 PublicationCurated
    Sequence conflicti291 – 2911Missing in CAA23474. 1 PublicationCurated
    Sequence conflicti394 – 3941F → L in CAA23474. 1 PublicationCurated
    Sequence conflicti415 – 4151P → H in CAA23474. 1 PublicationCurated
    Sequence conflicti441 – 4433GNE → VQ in CAA23474. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00171 Genomic DNA. Translation: CAA23474.1.
    Z11973 Genomic DNA. Translation: CAA78027.1.
    X86563 Genomic DNA. Translation: CAA60294.1.
    PIRiA01093. RKZML.
    S58560.
    RefSeqiNP_043033.1. NC_001666.2.

    Genome annotation databases

    GeneIDi845212.
    KEGGizma:845212.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00171 Genomic DNA. Translation: CAA23474.1 .
    Z11973 Genomic DNA. Translation: CAA78027.1 .
    X86563 Genomic DNA. Translation: CAA60294.1 .
    PIRi A01093. RKZML.
    S58560.
    RefSeqi NP_043033.1. NC_001666.2.

    3D structure databases

    ProteinModelPortali P00874.
    SMRi P00874. Positions 11-476.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P00874.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 845212.
    KEGGi zma:845212.

    Organism-specific databases

    Gramenei P00874.
    MaizeGDBi 69185.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.

    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. "Chloroplast gene sequence for the large subunit of ribulose bisphosphatecarboxylase of maize."
      McIntosh L., Poulsen C., Bogorad L.
      Nature 288:556-560(1980)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Relative rates of nucleotide substitution at the rbcL locus of monocotyledonous plants."
      Gaut B.S., Muse S.V., Clark W.D., Clegg M.T.
      J. Mol. Evol. 35:292-303(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leaf.
    3. "Complete sequence of the maize chloroplast genome: gene content, hotspots of divergence and fine tuning of genetic information by transcript editing."
      Maier R.M., Neckermann K., Igloi G.L., Koessel H.
      J. Mol. Biol. 251:614-628(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. B73.

    Entry informationi

    Entry nameiRBL_MAIZE
    AccessioniPrimary (citable) accession number: P00874
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 102 of the entry and version 2 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".UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3