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)

Q9ZHZ1

- RBL1_THIK1

UniProt

Q9ZHZ1 - RBL1_THIK1

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thiomonas intermedia (strain K12) (Thiobacillus intermedius)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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. 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 sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
    Binding sitei166 – 1661SubstrateUniRule annotation
    Active sitei168 – 1681Proton acceptorUniRule annotation
    Binding sitei170 – 1701SubstrateUniRule annotation
    Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
    Metal bindingi196 – 1961MagnesiumUniRule annotation
    Metal bindingi197 – 1971MagnesiumUniRule annotation
    Active sitei287 – 2871Proton acceptorUniRule annotation
    Binding sitei288 – 2881SubstrateUniRule annotation
    Binding sitei320 – 3201SubstrateUniRule annotation
    Sitei327 – 3271Transition state stabilizerUniRule annotation
    Binding sitei372 – 3721SubstrateUniRule 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. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Calvin cycle, Carbon dioxide fixation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciTINT75379:GH6C-115-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
    Ordered Locus Names:Tint_0115
    OrganismiThiomonas intermedia (strain K12) (Thiobacillus intermedius)
    Taxonomic identifieri75379 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesThiomonas
    ProteomesiUP000002185: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473Ribulose bisphosphate carboxylase large chainPRO_0000062659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei194 – 1941N6-carboxylysineUniRule annotation

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZHZ1.
    SMRiQ9ZHZ1. Positions 16-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000230831.
    KOiK01601.

    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: Complete.

    Q9ZHZ1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVKTYQAGV KEYRQTYWMP EYTPLDTDLL ACFKITPQAG VDREEAAAAV    50
    AAESSTGTWT TVWTDLLTDM DYYKGRAYRI EDVPGDDTCF YAFIAYPIDL 100
    FEEGSVVNVF TSLVGNVFGF KAIRALRLED IRFPIAYVKT CNGPPNGIQV 150
    ERDVINKYGR PLLGCTIKPK LGLSGKNYGR AVYECLRGGL DFTKDDENIN 200
    SQPFMRWKQR FDFVQEATLK AEQETGERKG HYLNVTAPTP DEMFKRAEYA 250
    KEIGAPIIMH DYITGGFCAN TGLAQWCRDN GMLLHIHRAM HAVLDRNPHH 300
    GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESYVPED 350
    RSRGIFFDQD WGSMPGAFAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL 400
    GHPWGNAAGA AANRVALEAC VQARNEGRQV EKEGREILTA AAQHSPELKI 450
    AMETWKEIKF EFDTVDKLDV TNK 473
    Length:473
    Mass (Da):52,787
    Last modified:May 1, 1999 - v1
    Checksum:i46EAF8F4C060ADF4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF046933 Genomic DNA. Translation: AAD02445.1.
    CP002021 Genomic DNA. Translation: ADG29528.1.
    RefSeqiYP_003641858.1. NC_014153.1.

    Genome annotation databases

    EnsemblBacteriaiADG29528; ADG29528; Tint_0115.
    GeneIDi9150845.
    KEGGitin:Tint_0115.
    PATRICi38290688. VBIThiInt85915_0120.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF046933 Genomic DNA. Translation: AAD02445.1 .
    CP002021 Genomic DNA. Translation: ADG29528.1 .
    RefSeqi YP_003641858.1. NC_014153.1.

    3D structure databases

    ProteinModelPortali Q9ZHZ1.
    SMRi Q9ZHZ1. Positions 16-460.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADG29528 ; ADG29528 ; Tint_0115 .
    GeneIDi 9150845.
    KEGGi tin:Tint_0115.
    PATRICi 38290688. VBIThiInt85915_0120.

    Phylogenomic databases

    HOGENOMi HOG000230831.
    KOi K01601.

    Enzyme and pathway databases

    BioCyci TINT75379:GH6C-115-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 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.

    Entry informationi

    Entry nameiRBL1_THIK1
    AccessioniPrimary (citable) accession number: Q9ZHZ1
    Secondary accession number(s): D5X330
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 72 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3