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Q8THG2

- RBL_METAC

UniProt

Q8THG2 - RBL_METAC

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      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.1 PublicationUniRule annotation
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.1 PublicationUniRule annotation

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotation

    Enzyme regulationi

    Reversibly inhibited by O2.1 Publication

    Temperature dependencei

    Active from 25 to 40 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei151 – 1511Proton acceptorUniRule annotation
    Binding sitei153 – 1531SubstrateUniRule annotation
    Metal bindingi177 – 1771Magnesium; via carbamate groupUniRule annotation
    Metal bindingi179 – 1791MagnesiumUniRule annotation
    Metal bindingi180 – 1801MagnesiumUniRule annotation
    Active sitei270 – 2701Proton acceptorUniRule annotation
    Binding sitei271 – 2711SubstrateUniRule annotation
    Binding sitei303 – 3031SubstrateUniRule annotation
    Sitei310 – 3101Transition state stabilizerUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase, Oxidoreductase

    Keywords - Biological processi

    Carbon dioxide fixation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMACE188937:GI2O-4613-MONOMER.

    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:MA_4555
    OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
    Taxonomic identifieri188937 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
    ProteomesiUP000002487: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Ribulose bisphosphate carboxylasePRO_0000062672Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei177 – 1771N6-carboxylysineUniRule annotation

    Proteomic databases

    PRIDEiQ8THG2.

    Interactioni

    Subunit structurei

    Homodimer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.1 Publication

    Protein-protein interaction databases

    STRINGi188937.MA4555.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8THG2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni354 – 3563Substrate bindingUniRule annotation
    Regioni376 – 3794Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1850.
    KOiK01601.
    OMAiFTQDWAS.
    PhylomeDBiQ8THG2.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01133. RuBisCO_L_type3.
    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.

    Q8THG2-1 [UniParc]FASTAAdd to Basket

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    MRRDYVDPGY SPKDTDLICE FHIEPAAGIS FEEASTHMAG ESSIDSWTEI    50
    STLSPELAAR LKPHVFYLDA DTQTVRVAYS EDLFELGSVP QVLSAVAGNI 100
    FSMKIVDNLR LQDITFPKSM LREFEGPNFG LPGVRDIVGV KDRPLVGTIV 150
    KPKVGLTSEM HAEVAYNAFA GGCDLVKDDE NLTDQKFNGF EKRAELTLKI 200
    AEKAEAETGE RKMYLCNITA PTCEEMIRRL HVLKDLGASY AMIDIVPTGW 250
    TALQTLREAA ADEGLALHAH RCMHSAFTRN PRHGVSMLLV AKLCRLIGLD 300
    QLHIGTVVGK MHGDKDEVLS IRDECVLDTV PADPEQHVLA QDWGGLKPMF 350
    PVASGGLAPT MIPDLYSIFG KEVIMQFGGG IHAHPMGTAA GAAACRQALE 400
    ASLEGISLQD YAKDHKELEA ALGKWLEK 428
    Length:428
    Mass (Da):46,787
    Last modified:June 1, 2002 - v1
    Checksum:iB03BFCBD9E8AFED5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010299 Genomic DNA. Translation: AAM07894.1.
    RefSeqiNP_619414.1. NC_003552.1.

    Genome annotation databases

    EnsemblBacteriaiAAM07894; AAM07894; MA_4555.
    GeneIDi1476449.
    KEGGimac:MA4555.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010299 Genomic DNA. Translation: AAM07894.1 .
    RefSeqi NP_619414.1. NC_003552.1.

    3D structure databases

    ProteinModelPortali Q8THG2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 188937.MA4555.

    Proteomic databases

    PRIDEi Q8THG2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM07894 ; AAM07894 ; MA_4555 .
    GeneIDi 1476449.
    KEGGi mac:MA4555.

    Phylogenomic databases

    eggNOGi COG1850.
    KOi K01601.
    OMAi FTQDWAS.
    PhylomeDBi Q8THG2.

    Enzyme and pathway databases

    BioCyci MACE188937:GI2O-4613-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01133. RuBisCO_L_type3.
    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. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
      Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
      , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
      Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
    2. "Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea."
      Finn M.W., Tabita F.R.
      J. Bacteriol. 185:3049-3059(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

    Entry informationi

    Entry nameiRBL_METAC
    AccessioniPrimary (citable) accession number: Q8THG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    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 proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3