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D5AUD5

- RBL2_RHOCB

UniProt

D5AUD5 - RBL2_RHOCB

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (15 Jun 2010)
      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 By similarity.By similarity

    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.By similarity

    Sites

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

    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. 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

    BioCyciRCAP272942:GJIY-1854-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase (EC:4.1.1.39)
    Short name:
    RuBisCO
    Gene namesi
    Name:cbbM
    Ordered Locus Names:RCAP_rcc01829
    OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
    Taxonomic identifieri272942 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
    ProteomesiUP000002361: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Ribulose bisphosphate carboxylasePRO_0000410720Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei191 – 1911N6-carboxylysineBy similarity

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliD5AUD5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiAKEHREF.

    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.

    D5AUD5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDQSNRYARL DLKEADLIAG GRHVLCAYVM KPKAGYGYLE TAAHFAAESS    50
    TGTNVEVSTT DDFTRGVDAL VYEIDPEKEI MKIAYPVELF DRNIIDGRAM 100
    LCSFLTLTIG NNQGMGDVEY AKMHEFYVPP CYLRLFDGPS MNIADMWRVL 150
    GRPVVDGGMV VGTIIKPKLG LRPKPFADAC YEFWLGGDFI KNDEPQGNQT 200
    FAPLKETIRL VADAMKRAQD ETGEAKLFSA NITADDHYEM VARGEYILET 250
    FGENADHVAF LVDGYVTGPA AITTARRQFP RQFLHYHRAG HGAVTSPQSM 300
    RGYTAFVLSK MSRLQGASGI HTGTMGYGKM EGDASDKIMA YMLTDEAAQG 350
    PFYHQDWLGM KATTPIISGG MNALRLPGFF DNLGHSNVIQ TSGGGAFGHL 400
    DGGTAGAKSL RQSCDAWKAG VDLVTYAKSH RELARAFESF PNDADKLYPG 450
    WRVALGVN 458
    Length:458
    Mass (Da):50,205
    Last modified:June 15, 2010 - v1
    Checksum:iA03E0FF321EF3B6C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001312 Genomic DNA. Translation: ADE85574.1.
    RefSeqiWP_013067553.1. NC_014034.1.
    YP_003577981.1. NC_014034.1.

    Genome annotation databases

    EnsemblBacteriaiADE85574; ADE85574; RCAP_rcc01829.
    GeneIDi9004652.
    KEGGircp:RCAP_rcc01829.
    PATRICi35503806. VBIRhoCap134200_1861.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001312 Genomic DNA. Translation: ADE85574.1 .
    RefSeqi WP_013067553.1. NC_014034.1.
    YP_003577981.1. NC_014034.1.

    3D structure databases

    ProteinModelPortali D5AUD5.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADE85574 ; ADE85574 ; RCAP_rcc01829 .
    GeneIDi 9004652.
    KEGGi rcp:RCAP_rcc01829.
    PATRICi 35503806. VBIRhoCap134200_1861.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi AKEHREF.

    Enzyme and pathway databases

    BioCyci RCAP272942:GJIY-1854-MONOMER.

    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. "Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
      Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
      J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
    2. "Expression of the cbbLcbbS and cbbM genes and distinct organization of the cbb Calvin cycle structural genes of Rhodobacter capsulatus."
      Paoli G.C., Morgan N.S., Tabita F.R., Shively J.M.
      Arch. Microbiol. 164:396-405(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: OPERON ORGANIZATION, EXPRESSION IN R.SPHAEROIDES.
      Strain: ATCC BAA-309 / NBRC 16581 / SB1003.

    Entry informationi

    Entry nameiRBL2_RHOCB
    AccessioniPrimary (citable) accession number: D5AUD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 28, 2011
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 27 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3