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A9BEH3

- RBL_PROM4

UniProt

A9BEH3 - RBL_PROM4

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Prochlorococcus marinus (strain MIT 9211)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      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 sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
    Binding sitei165 – 1651SubstrateUniRule annotation
    Active sitei167 – 1671Proton acceptorUniRule annotation
    Binding sitei169 – 1691SubstrateUniRule annotation
    Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Active sitei286 – 2861Proton acceptorUniRule annotation
    Binding sitei287 – 2871SubstrateUniRule annotation
    Binding sitei319 – 3191SubstrateUniRule annotation
    Sitei326 – 3261Transition state stabilizerUniRule annotation
    Binding sitei371 – 3711SubstrateUniRule 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

    Enzyme and pathway databases

    BioCyciPMAR93059:GHJV-571-MONOMER.

    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:cbbLUniRule annotation
    Synonyms:rbcLUniRule annotation
    Ordered Locus Names:P9211_05521
    OrganismiProchlorococcus marinus (strain MIT 9211)
    Taxonomic identifieri93059 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000000788: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Ribulose bisphosphate carboxylase large chainPRO_1000142751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei193 – 1931N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi93059.P9211_05521.

    Structurei

    3D structure databases

    ProteinModelPortaliA9BEH3.
    SMRiA9BEH3. Positions 15-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.
    OrthoDBiEOG6ZKXMS.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01338. RuBisCO_L_type1.
    InterProiIPR020888. 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.

    Sequencei

    Sequence statusi: Complete.

    A9BEH3-1 [UniParc]FASTAAdd to Basket

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    MSKKYDAGVK EYRDTYWTPE YVPLDTDLLA CFKCTGQEGV PREEVAAAVA    50
    AESSTGTWST VWSELLTDLE FYKGRCYRIE DVPGDKESFY AFIAYPLDLF 100
    EEGSITNVLT SLVGNVFGFK ALRHLRLEDI RFPMAFIKTC GGPPNGIVVE 150
    RDRLNKYGRP LLGCTIKPKL GLSGKNYGRV VYECLRGGLD LTKDDENINS 200
    QPFQRWRERF EFVAEAVKLA QQETGEVKGH YLNCTATTPE EMYERAEFAK 250
    ELDMPIIMHD YITGGFTANT GLANWCRKNG MLLHIHRAMH AVIDRHPKHG 300
    IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDN LRESFVPEDR 350
    TRGNFFDQDW GSMPGVFAVA SGGIHVWHMP ALLAIFGDDS CLQFGGGTHG 400
    HPWGSAAGAA ANRVALEACV KARNAGREIE KESRDILMEA AKHSPELAIA 450
    LETWKEIKFE FDTVDKLDVQ 470
    Length:470
    Mass (Da):52,601
    Last modified:January 15, 2008 - v1
    Checksum:i9590E77ECAE4F3F5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000878 Genomic DNA. Translation: ABX08483.1.
    RefSeqiWP_012195105.1. NC_009976.1.
    YP_001550437.1. NC_009976.1.

    Genome annotation databases

    EnsemblBacteriaiABX08483; ABX08483; P9211_05521.
    GeneIDi5731046.
    KEGGipmj:P9211_05521.
    PATRICi22986598. VBIProMar136502_0582.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000878 Genomic DNA. Translation: ABX08483.1 .
    RefSeqi WP_012195105.1. NC_009976.1.
    YP_001550437.1. NC_009976.1.

    3D structure databases

    ProteinModelPortali A9BEH3.
    SMRi A9BEH3. Positions 15-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 93059.P9211_05521.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX08483 ; ABX08483 ; P9211_05521 .
    GeneIDi 5731046.
    KEGGi pmj:P9211_05521.
    PATRICi 22986598. VBIProMar136502_0582.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PMAR93059:GHJV-571-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 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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MIT 9211.

    Entry informationi

    Entry nameiRBL_PROM4
    AccessioniPrimary (citable) accession number: A9BEH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 43 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3