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A2SJJ7

- RBL1B_METPP

UniProt

A2SJJ7 - RBL1B_METPP

Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

Organism
Methylibium petroleiphilum (strain PM1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      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.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 sitei125 – 1251Substrate; in homodimeric partnerUniRule annotation
    Binding sitei175 – 1751SubstrateUniRule annotation
    Active sitei177 – 1771Proton acceptorUniRule annotation
    Binding sitei179 – 1791SubstrateUniRule annotation
    Metal bindingi203 – 2031Magnesium; via carbamate groupUniRule annotation
    Metal bindingi205 – 2051MagnesiumUniRule annotation
    Metal bindingi206 – 2061MagnesiumUniRule annotation
    Active sitei295 – 2951Proton acceptorUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Sitei335 – 3351Transition state stabilizerUniRule annotation
    Binding sitei380 – 3801SubstrateUniRule 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. 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

    BioCyciMPET420662:GHBE-2816-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain 2UniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunit 2UniRule annotation
    Gene namesi
    Name:cbbL2UniRule annotation
    Ordered Locus Names:Mpe_A2782
    OrganismiMethylibium petroleiphilum (strain PM1)
    Taxonomic identifieri420662 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
    ProteomesiUP000000366: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Ribulose bisphosphate carboxylase large chain 2PRO_0000299965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi420662.Mpe_A2782.

    Structurei

    3D structure databases

    ProteinModelPortaliA2SJJ7.
    SMRiA2SJJ7. Positions 23-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OrthoDBiEOG6ZKXMS.

    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.

    A2SJJ7-1 [UniParc]FASTAAdd to Basket

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    MNEPTQITDT KKRYAAGVLK YAQMGYWNGD YVPKDTDILA LFRITPQDGV    50
    DPIEAAAAVA GESSTATWTV VWTDRLTACD MYRAKAYKVE PVPNNPGQYF 100
    CYVAYDLSLF EEGSIANVTA SIIGNVFSFK PLKAARLEDM KFPVSYVKTF 150
    AGPPTGIVVE RERLDKFGRP LLGATTKPKL GLSGRNYGRV VYEGLKGGLD 200
    FMKDDENINS QPFMHWRDRF LFVMDAVNKA SAATGEVKGS YLNVTAGTME 250
    EMYRRAEFAK ELGSVIIMID LVVGYTAIQS MSNWARQNDM VLHMHRAGHG 300
    TYTRQKNHGV SFRVIAKWLR MAGVDHLHTG TAVGKLEGDP LTVQGYYNVC 350
    RDTHTKVDLP RGIFFDQDWG ALKKVMPVAS GGIHAGQMHQ LIDLFGDDVV 400
    LQFGGGTIGH PQGIQAGATA NRVALEAMVL ARNEGRDIKN EGPQILRDAA 450
    KSCTPLAAAL DTWGDITFNY TSTDTSDYVP TPSVA 485
    Length:485
    Mass (Da):53,310
    Last modified:September 11, 2007 - v2
    Checksum:i3B36C71F79F2FCAD
    GO

    Sequence cautioni

    The sequence ABM95736.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000555 Genomic DNA. Translation: ABM95736.1. Different initiation.
    RefSeqiYP_001021971.1. NC_008825.1.

    Genome annotation databases

    EnsemblBacteriaiABM95736; ABM95736; Mpe_A2782.
    GeneIDi4785032.
    KEGGimpt:Mpe_A2782.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000555 Genomic DNA. Translation: ABM95736.1 . Different initiation.
    RefSeqi YP_001021971.1. NC_008825.1.

    3D structure databases

    ProteinModelPortali A2SJJ7.
    SMRi A2SJJ7. Positions 23-466.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 420662.Mpe_A2782.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM95736 ; ABM95736 ; Mpe_A2782 .
    GeneIDi 4785032.
    KEGGi mpt:Mpe_A2782.

    Phylogenomic databases

    eggNOGi COG1850.
    HOGENOMi HOG000230831.
    KOi K01601.
    OrthoDBi EOG6ZKXMS.

    Enzyme and pathway databases

    BioCyci MPET420662:GHBE-2816-MONOMER.

    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. "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
      Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
      J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PM1.

    Entry informationi

    Entry nameiRBL1B_METPP
    AccessioniPrimary (citable) accession number: A2SJJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 48 of the entry and version 2 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 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