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)

E4NPX6

- E4NPX6_HALBP

UniProt

E4NPX6 - E4NPX6_HALBP

Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 / PR3)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (08 Feb 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei156 – 1561Proton acceptorUniRule annotation
    Binding sitei158 – 1581SubstrateUniRule annotation
    Metal bindingi182 – 1821Magnesium; via carbamate groupUniRule annotation
    Metal bindingi184 – 1841MagnesiumUniRule annotation
    Metal bindingi185 – 1851MagnesiumUniRule annotation
    Active sitei274 – 2741Proton acceptorUniRule annotation
    Binding sitei275 – 2751SubstrateUniRule annotation
    Binding sitei307 – 3071SubstrateUniRule annotation
    Sitei315 – 3151Transition 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 annotationImported, OxidoreductaseUniRule annotation

    Keywords - Biological processi

    Carbon dioxide fixationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Enzyme and pathway databases

    BioCyciHBOR469382:GCNS-2156-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 annotationImported
    Ordered Locus Names:Hbor_21570Imported
    ORF Names:C499_17644Imported
    OrganismiHalogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 / PR3)Imported
    Taxonomic identifieri469382 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalogeometricum
    ProteomesiUP000006663: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei182 – 1821N6-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

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni343 – 3453Substrate bindingUniRule annotation
    Regioni365 – 3684Substrate 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

    HOGENOMiHOG000230831.
    KOiK01601.
    OMAiFTQDWAS.

    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.

    E4NPX6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGITYEDFL DLSYEPDESD LVCTFRIAPA EGMDVEAAAS RVASESSNGT    50
    WAALPTGEGF TDMGATTFDI RGSDDSAEVD VAYPAGLFEP GSMPQILSCI 100
    AGNIMGMKAV DTIRLADCQW PEALVSSFAG PQFGSSVREE IFGIEEDRPI 150
    LATVPKPKVG LSTDRHAEVG YEAWLGGVDL LKDDENLTDQ SFNPYHDRLV 200
    ESLALRDDAE DETGEKKSYL INVTADTNTM LERVDLAAEE GCEYVMVDVI 250
    TTGWAAVQTV RERCEDHGIA IHAHRAMHAA FDRLENHGVS MRVLAQISRL 300
    CGVDQLHTGT AGLGKLANED TVGINDWMRS ELYGLNDVLP VASGGLHPGL 350
    IPDLLDATGT NVCVQAGGGI HGHPDGTRAG AAALRAAVDG YAAGKSLEES 400
    ADDSPELATA IDEWGTETPR 420
    Length:420
    Mass (Da):44,775
    Last modified:February 8, 2011 - v1
    Checksum:i4CF3B80193853A63
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001690 Genomic DNA. Translation: ADQ67721.1.
    AOHT01000051 Genomic DNA. Translation: ELY23598.1.
    RefSeqiWP_006056824.1. NZ_AOHT01000051.1.
    YP_004037166.1. NC_014729.1.

    Genome annotation databases

    EnsemblBacteriaiADQ67721; ADQ67721; Hbor_21570.
    ELY23598; ELY23598; C499_17644.
    GeneIDi9993976.
    KEGGihbo:Hbor_21570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001690 Genomic DNA. Translation: ADQ67721.1 .
    AOHT01000051 Genomic DNA. Translation: ELY23598.1 .
    RefSeqi WP_006056824.1. NZ_AOHT01000051.1.
    YP_004037166.1. NC_014729.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADQ67721 ; ADQ67721 ; Hbor_21570 .
    ELY23598 ; ELY23598 ; C499_17644 .
    GeneIDi 9993976.
    KEGGi hbo:Hbor_21570.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.
    OMAi FTQDWAS.

    Enzyme and pathway databases

    BioCyci HBOR469382:GCNS-2156-MONOMER.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700274 / DSM 11551 / JCM 10706 / PR3Imported and PR 3Imported.
    2. Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A., Eisen J.A., Facciotti M.T.
      Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: DSM 11551Imported.

    Entry informationi

    Entry nameiE4NPX6_HALBP
    AccessioniPrimary (citable) accession number: E4NPX6
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 8, 2011
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 27 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 proteome, Reference proteomeImported

    External Data

    Dasty 3