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O98949

- O98949_9RHOD

UniProt

O98949 - O98949_9RHOD

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Galdieria partita
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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 sitei74 – 741Sulfate 1
    Binding sitei132 – 1321Substrate; in homodimeric partnerUniRule annotation
    Binding sitei182 – 1821SubstrateUniRule annotation
    Active sitei184 – 1841Proton acceptorUniRule annotation
    Binding sitei184 – 1841Sulfate 2
    Binding sitei186 – 1861SubstrateUniRule annotation
    Metal bindingi210 – 2101MagnesiumImported
    Metal bindingi210 – 2101Magnesium; via carbamate groupUniRule annotation
    Metal bindingi212 – 2121MagnesiumUniRule annotationImported
    Metal bindingi212 – 2121Magnesium
    Metal bindingi213 – 2131MagnesiumUniRule annotationImported
    Metal bindingi213 – 2131Magnesium
    Active sitei302 – 3021Proton acceptorUniRule annotation
    Binding sitei303 – 3031SubstrateUniRule annotation
    Binding sitei335 – 3351SubstrateUniRule annotation
    Binding sitei342 – 3421Sulfate 2
    Sitei342 – 3421Transition state stabilizerUniRule annotation
    Binding sitei387 – 3871SubstrateUniRule annotation
    Binding sitei389 – 3891Sulfate 2; via amide nitrogen

    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

    LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotationImported, Metal-bindingUniRule annotationImported

    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; ChloroplastImported
    OrganismiGaldieria partitaImported
    Taxonomic identifieri83374 [NCBI]
    Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeGaldieria

    Subcellular locationi

    Plastidchloroplast UniRule annotation

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    ChloroplastUniRule annotationImported, Plastid

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei210 – 2101N6-carboxylysineUniRule annotationImported
    Modified residuei210 – 2101N6-carboxylysine

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BWVX-ray2.40A/C/E/G1-493[»]
    1IWAX-ray2.60A/C/E/G/I/K/M/O1-493[»]
    ProteinModelPortaliO98949.
    SMRiO98949. Positions 14-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO98949.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni411 – 4122Sulfate 2 binding

    Sequence similaritiesi

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

    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.

    O98949-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQSIEEKSV QERTRIKNSR YESGVIPYAK MGYWNPDYQV KDTDVLALFR    50
    VTPQPGVDPI EAAAAVAGES STATWTVVWT DLLTAADLYR AKAYKVDQVP 100
    NNPEQYFAYI AYELDLFEEG SIANLTASII GNVFGFKAVK ALRLEDMRLP 150
    LAYLKTFQGP ATGVILERER LDKFGRPLLG CTTKPKLGLS GKNYGRVVYE 200
    ALKGGLDFVK DDENINSQPF MRWRERYLFT MEAVNKASAA TGEVKGHYLN 250
    VTAATMEEMY ARANFAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH 300
    LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT 350
    RGFYKTLLLP KLERNLQEGL FFDMEWASLR KVMPVASGGI HAGQMHQLIH 400
    YLGEDVVLQF GGGTIGHPDG IQAGATANRV ALEAMILARN ENRDYLTEGP 450
    EILREAAKTC GALRTALDLW KDITFNYTST DTSDFVETPT ANI 493
    Length:493
    Mass (Da):54,994
    Last modified:May 1, 1999 - v1
    Checksum:iFF86E3FF8C68C937
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018008 Genomic DNA. Translation: BAA75796.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018008 Genomic DNA. Translation: BAA75796.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BWV X-ray 2.40 A/C/E/G 1-493 [» ]
    1IWA X-ray 2.60 A/C/E/G/I/K/M/O 1-493 [» ]
    ProteinModelPortali O98949.
    SMRi O98949. Positions 14-486.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei O98949.

    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. "Structure and function study of ribulose-1,5-bisphosphate carboxylase/oxygenase of the red algae, Galdieria partita Tokara."
      Tomizawa K.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita."
      Sugawara H., Yamamoto H., Shibata N., Inoue T., Okada S., Miyake C., Yokota A., Kai Y.
      J. Biol. Chem. 274:15655-15661(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, CARBOXYLATION AT LYS-210.
    3. "X-ray structure of Galdieria Rubisco complexed with one sulfate ion per active site."
      Okano Y., Mizohata E., Xie Y., Matsumura H., Sugawara H., Inoue T., Yokota A., Kai Y.
      FEBS Lett. 527:33-36(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).

    Entry informationi

    Entry nameiO98949_9RHOD
    AccessioniPrimary (citable) accession number: O98949
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 1, 1999
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    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

    3D-structureImported

    External Data

    Dasty 3