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L0HPH2

- L0HPH2_ACIS0

UniProt

L0HPH2 - L0HPH2_ACIS0

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Aciduliprofundum sp. (strain MAR08-339)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 10 (01 Oct 2014)
      Sequence version 1 (06 Mar 2013)
      Previous versions | rss
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    Functioni

    Catalyzes the addition of molecular CO2 and H2O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.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
    Active sitei149 – 1491Proton acceptorUniRule annotation
    Binding sitei151 – 1511SubstrateUniRule annotation
    Metal bindingi175 – 1751Magnesium; via carbamate groupUniRule annotation
    Metal bindingi177 – 1771MagnesiumUniRule annotation
    Metal bindingi178 – 1781MagnesiumUniRule annotation
    Active sitei265 – 2651Proton acceptorUniRule annotation
    Binding sitei266 – 2661SubstrateUniRule annotation
    Binding sitei298 – 2981SubstrateUniRule annotation
    Sitei305 – 3051Transition state stabilizerUniRule annotation

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB-HAMAP
    2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. AMP catabolic process Source: UniProtKB-HAMAP
    2. carbon fixation Source: InterPro

    Keywords - Molecular functioni

    LyaseUniRule annotation, OxidoreductaseUniRule annotation

    Keywords - Biological processi

    Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCOUniRule annotation
    Gene namesi
    Name:rbcLUniRule annotation
    Ordered Locus Names:AciM339_1392Imported
    OrganismiAciduliprofundum sp. (strain MAR08-339)Imported
    Taxonomic identifieri673860 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaAciduliprofundum
    ProteomesiUP000010814: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei175 – 1751N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliL0HPH2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni347 – 3493Substrate bindingUniRule annotation
    Regioni369 – 3724Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01601.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    InterProiIPR017712. RuBisCO_III.
    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.
    TIGRFAMsiTIGR03326. rubisco_III. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    L0HPH2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTYIELDYEP KDTDLLVWFY AEPPAGRDMK YVADRIAEES SIGTWTDLKT    50
    LLPEIWEKLR ARVYEIDEER RYVKIAYSLH LFEVKNMPAI LASVAGNVFG 100
    MKSVENLRVL DTRFPLELLS EYPGPKYGVQ GVREMTGVRD RPFLGTIIKP 150
    KIGLPAKMHA EVAYEAWVGG LDIVKDDENL ASQDFNRFEE RLSLTLEKKD 200
    LAEEETGEKK IYLVNITAPY REMIRRAELV QDAGNEFVMI DVFISGFSAV 250
    QSYREEGFKM AIHAHRAMHA AITRNPRHGI TMLALAKIYR VLGVDNLHIG 300
    TAVGKMEGSA AEVSAIREEI QMGNVPANDT RFQQSWGDIK PVLAVASGGL 350
    HPGHVPAVVD ILGKDIVIQA GGGVHGHPEG TRKGATAMRQ ALEAKMQGIS 400
    LQEYAKDHEE LRKALEKFVK 420
    Length:420
    Mass (Da):47,034
    Last modified:March 6, 2013 - v1
    Checksum:i93D0CBD4908AC61B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003168 Genomic DNA. Translation: AGB05248.1.
    RefSeqiWP_015283871.1. NC_019942.1.
    YP_007247414.1. NC_019942.1.

    Genome annotation databases

    EnsemblBacteriaiAGB05248; AGB05248; AciM339_1392.
    GeneIDi14306529.
    KEGGiacf:AciM339_1392.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003168 Genomic DNA. Translation: AGB05248.1 .
    RefSeqi WP_015283871.1. NC_019942.1.
    YP_007247414.1. NC_019942.1.

    3D structure databases

    ProteinModelPortali L0HPH2.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AGB05248 ; AGB05248 ; AciM339_1392 .
    GeneIDi 14306529.
    KEGGi acf:AciM339_1392.

    Phylogenomic databases

    KOi K01601.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    InterProi IPR017712. RuBisCO_III.
    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.
    TIGRFAMsi TIGR03326. rubisco_III. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of Aciduliprofundum sp. MAR08-339."
      Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Flores G., Reysenbach A.-L., Woyke T.
      Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MAR08-339Imported.

    Entry informationi

    Entry nameiL0HPH2_ACIS0
    AccessioniPrimary (citable) accession number: L0HPH2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 6, 2013
    Last sequence update: March 6, 2013
    Last modified: October 1, 2014
    This is version 10 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Miscellaneous

    Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O2 to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains.UniRule annotation

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3