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P23755

- RBL_GALSU

UniProt

P23755 - RBL_GALSU

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Galdieria sulphuraria (Red alga)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      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 sitei132 – 1321Substrate; in homodimeric partnerUniRule annotation
    Binding sitei182 – 1821SubstrateUniRule annotation
    Active sitei184 – 1841Proton acceptorUniRule annotation
    Binding sitei186 – 1861SubstrateUniRule annotation
    Metal bindingi210 – 2101Magnesium; via carbamate groupUniRule annotation
    Metal bindingi212 – 2121MagnesiumUniRule annotation
    Metal bindingi213 – 2131MagnesiumUniRule annotation
    Active sitei302 – 3021Proton acceptorUniRule annotation
    Binding sitei303 – 3031SubstrateUniRule annotation
    Binding sitei335 – 3351SubstrateUniRule annotation
    Sitei342 – 3421Transition state stabilizerUniRule annotation
    Binding sitei387 – 3871SubstrateUniRule 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
    OrganismiGaldieria sulphuraria (Red alga)
    Taxonomic identifieri130081 [NCBI]
    Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeGaldieria

    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
    Chaini1 – 493493Ribulose bisphosphate carboxylase large chainPRO_0000062476Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-60089N.

    Structurei

    Secondary structure

    1
    493
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 335
    Beta strandi45 – 539
    Helixi59 – 6911
    Helixi79 – 835
    Helixi86 – 894
    Beta strandi92 – 998
    Beta strandi102 – 11211
    Helixi114 – 1163
    Helixi122 – 1309
    Helixi133 – 1353
    Turni136 – 1383
    Beta strandi139 – 14810
    Helixi151 – 1544
    Helixi163 – 1719
    Beta strandi178 – 1825
    Beta strandi184 – 1874
    Helixi191 – 20414
    Beta strandi207 – 2104
    Beta strandi216 – 2183
    Helixi223 – 24119
    Beta strandi246 – 2505
    Helixi256 – 26914
    Beta strandi272 – 2776
    Helixi278 – 2803
    Helixi282 – 29413
    Beta strandi298 – 3025
    Turni304 – 3063
    Helixi307 – 3104
    Beta strandi311 – 3177
    Helixi319 – 32911
    Beta strandi332 – 3354
    Beta strandi339 – 3413
    Helixi347 – 35812
    Beta strandi360 – 3623
    Turni366 – 3694
    Beta strandi383 – 3864
    Helixi392 – 3943
    Helixi395 – 4028
    Beta strandi407 – 4115
    Helixi412 – 4154
    Helixi421 – 44020
    Helixi445 – 45814
    Helixi461 – 4699
    Turni470 – 4734

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F0HX-ray1.96A1-493[»]
    4F0KX-ray2.05A1-493[»]
    4F0MX-ray2.25A1-493[»]
    ProteinModelPortaliP23755.
    SMRiP23755. Positions 14-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.

    P23755-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQSLEEKSV QERTRIKNSR YESGVIPYAK MGYWNPDYQV KDTDVLALFR    50
    VTPQPGVDPI EAAAAVAGES STATWTVVWT DLLTAADLYR AKAYKVDQVP 100
    NNPEQYFAYI AYELDLFEEG SIANLTASII GNVFGFKAVK ALRLEDMRLP 150
    FAYIKTFQGP ATGVILERER LDKFGRPLLG CTTKPKLGLS GKNYGRVVYE 200
    ALKGGLDFVK DDENINSQPF MRWRERYLFV MEAVNKAAAA TGEVKGHYLN 250
    VTAATMEEMY ARAQLAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH 300
    LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT 350
    RGFYKTLLLP KLERNLQEGL FFDMDWASLR KVMPVASGGI HAGQMHQLIH 400
    YLGEDVVLQF GGGTIGHPDG IQSGATANRV ALEAMILARN ENRDFLTEGP 450
    EILREAAKNC GALRTALDLW KDITFNYTST DTSDFVETPT ANI 493
    Length:493
    Mass (Da):54,989
    Last modified:November 1, 1991 - v1
    Checksum:iB69EE280D47C6FA2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55524 Genomic DNA. Translation: CAA39140.1.
    AF233069 Genomic DNA. Translation: AAF81681.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55524 Genomic DNA. Translation: CAA39140.1 .
    AF233069 Genomic DNA. Translation: AAF81681.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F0H X-ray 1.96 A 1-493 [» ]
    4F0K X-ray 2.05 A 1-493 [» ]
    4F0M X-ray 2.25 A 1-493 [» ]
    ProteinModelPortali P23755.
    SMRi P23755. Positions 14-486.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60089N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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 of the Rubisco operon from the unicellular red alga Cyanidium caldarium: evidence for a polyphyletic origin of the plastids."
      Valentin K.-U., Zetsche K.
      Mol. Gen. Genet. 222:425-430(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 14-1-1 / Isolate 107.79/Goettingen.
    2. Whitney S.M., Andrews J.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: UTEX 2393.

    Entry informationi

    Entry nameiRBL_GALSU
    AccessioniPrimary (citable) accession number: P23755
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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-structure

    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