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A2SFV1

- RBL1A_METPP

UniProt

A2SFV1 - RBL1A_METPP

Protein

Ribulose bisphosphate carboxylase large chain 1

Gene

cbbL1

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 1 (06 Mar 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 sitei128 – 1281Substrate; in homodimeric partnerUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Active sitei180 – 1801Proton acceptorUniRule annotation
    Binding sitei182 – 1821SubstrateUniRule annotation
    Metal bindingi206 – 2061Magnesium; via carbamate groupUniRule annotation
    Metal bindingi208 – 2081MagnesiumUniRule annotation
    Metal bindingi209 – 2091MagnesiumUniRule annotation
    Active sitei298 – 2981Proton acceptorUniRule annotation
    Binding sitei299 – 2991SubstrateUniRule annotation
    Binding sitei331 – 3311SubstrateUniRule annotation
    Sitei338 – 3381Transition state stabilizerUniRule annotation
    Binding sitei383 – 3831SubstrateUniRule 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-1499-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chain 1UniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunit 1UniRule annotation
    Gene namesi
    Name:cbbL1UniRule annotation
    Ordered Locus Names:Mpe_A1478
    OrganismiMethylibium petroleiphilum (strain PM1)
    Taxonomic identifieri420662 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
    ProteomesiUP000000366: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 488488Ribulose bisphosphate carboxylase large chain 1PRO_0000299964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei206 – 2061N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi420662.Mpe_A1478.

    Structurei

    3D structure databases

    ProteinModelPortaliA2SFV1.
    SMRiA2SFV1. Positions 26-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiLDYYLEC.
    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.

    A2SFV1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKPMEDAAI TDVKKRYSAG VLKYRQMGYW MPDYVPKDTD TICLFRITPQ    50
    DGVDPVEAAA AVAGESSTAT WTVVWTDRLT ACDSYRAKAY KVEPVPGIPG 100
    QFFAWVAYDI ILFEEGSIAN MTASLIGNVF SFKPLKAARL EDIRIPVAYV 150
    KTFKGPPTGL VVERERLDKF GRPLLGATTK PKLGLSGRNY GRVVYEGLKG 200
    GLDFMKDDEN INSQPFMHWR DRYLYVMDAV NKASAATGEI KGSYLNVTAA 250
    TMEDMYERAE FAKELGSVIV MIDLVIGYTA IQSMSNWARR NDVILHLHRA 300
    GHGTYTRQKN HGVSFRVIAK WMRLAGVDHI HTGTAVGKLE GDPMTVQGYY 350
    NVCRDSVTKQ DLPRGLFFDQ DWADLKKVMP VASGGIHAGQ MHQLIDLFGD 400
    DVVLQFGGGT IGHPQGIQAG AVANRVALEC MVKARNEGRD IKNEGPEILR 450
    KAAQFCAPLK QALDTWGEIS FNYTPTDTSD YAVTPGVA 488
    Length:488
    Mass (Da):53,929
    Last modified:March 6, 2007 - v1
    Checksum:iD6FE45BF3D28E476
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000555 Genomic DNA. Translation: ABM94440.1.
    RefSeqiYP_001020675.1. NC_008825.1.

    Genome annotation databases

    EnsemblBacteriaiABM94440; ABM94440; Mpe_A1478.
    GeneIDi4784076.
    KEGGimpt:Mpe_A1478.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000555 Genomic DNA. Translation: ABM94440.1 .
    RefSeqi YP_001020675.1. NC_008825.1.

    3D structure databases

    ProteinModelPortali A2SFV1.
    SMRi A2SFV1. Positions 26-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 420662.Mpe_A1478.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM94440 ; ABM94440 ; Mpe_A1478 .
    GeneIDi 4784076.
    KEGGi mpt:Mpe_A1478.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci MPET420662:GHBE-1499-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 nameiRBL1A_METPP
    AccessioniPrimary (citable) accession number: A2SFV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 48 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 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