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P04718

- RBL2_RHORU

UniProt

P04718 - RBL2_RHORU

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodospirillum rubrum
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      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. 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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111Substrate; in homodimeric partner
    Active sitei166 – 1661Proton acceptor
    Binding sitei168 – 1681Substrate
    Metal bindingi191 – 1911Magnesium; via carbamate group
    Metal bindingi193 – 1931Magnesium
    Metal bindingi194 – 1941Magnesium
    Active sitei287 – 2871Proton acceptor
    Binding sitei288 – 2881Substrate
    Binding sitei321 – 3211Substrate
    Sitei329 – 3291Transition state stabilizer
    Binding sitei368 – 3681Substrate

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB-HAMAP
    2. monooxygenase activity Source: UniProtKB-KW
    3. ribulose-bisphosphate carboxylase activity Source: CACAO

    GO - Biological processi

    1. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation, Photosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13280.
    SABIO-RKP04718.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase (EC:4.1.1.39)
    Short name:
    RuBisCO
    Gene namesi
    Name:cbbM
    Synonyms:cbbL2, rbpL
    OrganismiRhodospirillum rubrum
    Taxonomic identifieri1085 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 466466Ribulose bisphosphate carboxylasePRO_0000062666Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei191 – 1911N6-carboxylysine1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP04718. 1 interaction.
    MINTiMINT-8090212.

    Structurei

    Secondary structure

    1
    466
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 63
    Helixi14 – 207
    Beta strandi23 – 3210
    Beta strandi34 – 363
    Helixi38 – 4811
    Turni49 – 513
    Beta strandi70 – 756
    Turni76 – 794
    Beta strandi80 – 867
    Helixi87 – 893
    Turni94 – 963
    Helixi101 – 1099
    Helixi111 – 1133
    Beta strandi116 – 12712
    Helixi130 – 1334
    Helixi143 – 1508
    Beta strandi154 – 1563
    Beta strandi160 – 1645
    Beta strandi166 – 1694
    Helixi173 – 18311
    Turni184 – 1863
    Beta strandi188 – 1914
    Beta strandi197 – 1993
    Helixi204 – 22219
    Beta strandi227 – 2315
    Helixi237 – 25115
    Helixi252 – 2576
    Beta strandi258 – 2636
    Turni264 – 2663
    Helixi269 – 27810
    Beta strandi284 – 2874
    Turni289 – 2913
    Helixi292 – 2954
    Beta strandi301 – 3033
    Helixi305 – 31511
    Beta strandi318 – 3214
    Helixi336 – 3449
    Beta strandi346 – 3494
    Beta strandi354 – 3563
    Beta strandi364 – 3696
    Turni373 – 3753
    Helixi376 – 3838
    Beta strandi389 – 3924
    Turni394 – 3974
    Helixi403 – 41917
    Helixi423 – 4286
    Helixi431 – 4399
    Helixi441 – 4477
    Helixi451 – 4555

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RBAX-ray2.60A/B1-466[»]
    1RUSX-ray2.90A/B1-466[»]
    2RUSX-ray2.30A/B1-466[»]
    5RUBX-ray1.70A/B1-466[»]
    9RUBX-ray2.60A/B1-466[»]
    ProteinModelPortaliP04718.
    SMRiP04718. Positions 2-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04718.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01339. RuBisCO_L_type2.
    InterProiIPR020871. RuBisCO.
    IPR020878. RuBisCo_large_chain_AS.
    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.

    P04718-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS    50
    TGTNVEVCTT DDFTRGVDAL VYEVDEAREL TKIAYPVALF HRNITDGKAM 100
    IASFLTLTMG NNQGMGDVEY AKMHDFYVPE AYRALFDGPS VNISALWKVL 150
    GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC HAFWLGGDFI KNDEPQGNQP 200
    FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI IARGEYVLET 250
    FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK 300
    RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG 350
    PFYRQSWGGM KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI 400
    DGPVAGARSL RQAWQAWRDG VPVLDYAREH KELARAFESF PGDADQIYPG 450
    WRKALGVEDT RSALPA 466
    Length:466
    Mass (Da):50,504
    Last modified:August 13, 1987 - v1
    Checksum:i37D8C0076CAF7D54
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00286 Genomic DNA. Translation: CAA25080.1.
    PIRiS07295.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00286 Genomic DNA. Translation: CAA25080.1 .
    PIRi S07295.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RBA X-ray 2.60 A/B 1-466 [» ]
    1RUS X-ray 2.90 A/B 1-466 [» ]
    2RUS X-ray 2.30 A/B 1-466 [» ]
    5RUB X-ray 1.70 A/B 1-466 [» ]
    9RUB X-ray 2.60 A/B 1-466 [» ]
    ProteinModelPortali P04718.
    SMRi P04718. Positions 2-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P04718. 1 interaction.
    MINTi MINT-8090212.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13280.
    SABIO-RK P04718.

    Miscellaneous databases

    EvolutionaryTracei P04718.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01339. RuBisCO_L_type2.
    InterProi IPR020871. RuBisCO.
    IPR020878. RuBisCo_large_chain_AS.
    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. "Nucleotide sequence of the ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum."
      Nargang F., McIntosh L., Somerville C.R.
      Mol. Gen. Genet. 193:220-224(1984)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Isolation and sequencing of an active-site peptide from Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase after affinity labeling with 2-[(bromoacetyl)amino]pentitol 1,5-bisphosphate."
      Fraij B., Hartman F.C.
      Biochemistry 22:1515-1520(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 314-337.
    3. "Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution."
      Schneider G., Lindqvist Y., Braenden C.-I., Lorimer G.
      EMBO J. 5:3409-3415(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    4. "Crystal structure of the active site of ribulose-bisphosphate carboxylase."
      Andersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T., Braenden C.-I., Lorimer G.H.
      Nature 337:229-234(1989)
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    5. "Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7-A resolution."
      Schneider G., Lindqvist Y., Lundqvist T.
      J. Mol. Biol. 211:989-1008(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    6. "Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution."
      Lundqvist T., Schneider G.
      Biochemistry 30:904-908(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), COFACTOR, SUBUNIT, CARBAMYLATION AT LYS-191.

    Entry informationi

    Entry nameiRBL2_RHORU
    AccessioniPrimary (citable) accession number: P04718
    Secondary accession number(s): P19365, P72313
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 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 contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity.By similarity

    Keywords - Technical termi

    3D-structure, 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