Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P28425

- RBL_HYDVI

UniProt

P28425 - RBL_HYDVI

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Hydrophyllum virginianum (Eastern waterleaf)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei114 – 1141Substrate; in homodimeric partnerUniRule annotation
    Binding sitei164 – 1641SubstrateUniRule annotation
    Active sitei166 – 1661Proton acceptorUniRule annotation
    Binding sitei168 – 1681SubstrateUniRule annotation
    Metal bindingi192 – 1921Magnesium; via carbamate groupUniRule annotation
    Metal bindingi194 – 1941MagnesiumUniRule annotation
    Metal bindingi195 – 1951MagnesiumUniRule annotation
    Active sitei285 – 2851Proton acceptorUniRule annotation
    Binding sitei286 – 2861SubstrateUniRule annotation
    Binding sitei318 – 3181SubstrateUniRule annotation
    Sitei325 – 3251Transition state stabilizerUniRule annotation
    Binding sitei370 – 3701SubstrateUniRule annotation

    GO - Molecular functioni

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

    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

    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:rbcLUniRule annotation
    Encoded oniPlastid; Chloroplast
    OrganismiHydrophyllum virginianum (Eastern waterleaf)
    Taxonomic identifieri4134 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesHydrophyllaceaeHydrophyllum

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 467›467Ribulose bisphosphate carboxylase large chainPRO_0000062494Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6,N6,N6-trimethyllysineUniRule annotation
    Modified residuei192 – 1921N6-carboxylysineUniRule annotation
    Disulfide bondi238 – 238Interchain; in linked formUniRule annotation

    Post-translational modificationi

    The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

    Keywords - PTMi

    Disulfide bond, Methylation

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP28425.
    SMRiP28425. Positions 1-454.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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: Fragment.

    P28425-1 [UniParc]FASTAAdd to Basket

    « Hide

    SVGFKAGVKE YKLTYYTPEY ETKDTDILAA FRVSPQPGVP PEEAGAAVAA    50
    ESSTGTWTTV WTDGLTNLDR YKGRCYHIDP VLGEEDQYIA YVAYPLDLFE 100
    EGSVTNMFTS IVGNVFGFKA LRALRLEDLR IPTAYVKTFQ GPPHGIQVER 150
    DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF TKDDENVNSQ 200
    PFMRWRDRLL FCAEAIFKSQ AETGEIKGHY LNATAGNCEE MMKRAVFARE 250
    LGVPIVMHDY LTGGFTANTT LASYCRDNGL LLHIHRAMHA VIDRQKNHGI 300
    HFRVLAKALR MSGGDHIHSG TVVGKLEGER NITLSFVVLL RDDYIEKDRS 350
    RGIFFTQDWV SLPGVLPVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH 400
    PWGNAPGAVA NRVSLEACVQ ARNEGRDLAR EGNDIIREAC KWSPELAAAC 450
    EVWKEIKFEF TDMDTLD 467
    Length:467
    Mass (Da):51,905
    Last modified:December 1, 1992 - v1
    Checksum:iAFD680117497BD9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01927 Genomic DNA. Translation: AAA84324.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01927 Genomic DNA. Translation: AAA84324.2 .

    3D structure databases

    ProteinModelPortali P28425.
    SMRi P28425. Positions 1-454.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Carnivorous plants: phylogeny and structural evolution."
      Albert V.A., Williams S.E., Chase M.W.
      Science 257:1491-1495(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiRBL_HYDVI
    AccessioniPrimary (citable) accession number: P28425
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3