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I0GCV3

- I0GCV3_9BRAD

UniProt

I0GCV3 - I0GCV3_9BRAD

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, S23_53970
Organism
Bradyrhizobium sp. S23321
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 By similarity.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 By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei175 – 1751Substrate By similarityUniRule annotation
Active sitei177 – 1771Proton acceptor By similarityUniRule annotation
Binding sitei179 – 1791Substrate By similarityUniRule annotation
Metal bindingi203 – 2031Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi205 – 2051Magnesium By similarityUniRule annotation
Metal bindingi206 – 2061Magnesium By similarityUniRule annotation
Active sitei295 – 2951Proton acceptor By similarityUniRule annotation
Binding sitei296 – 2961Substrate By similarityUniRule annotation
Binding sitei328 – 3281Substrate By similarityUniRule annotation
Sitei335 – 3351Transition state stabilizer By similarityUniRule annotation
Binding sitei380 – 3801Substrate By similarityUniRule 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
Complete GO annotation...

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciBSP335659:GL9K-5394-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 annotationImported
ORF Names:S23_53970Imported
OrganismiBradyrhizobium sp. S23321Imported
Taxonomic identifieri335659 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000007886: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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.

I0GCV3-1 [UniParc]FASTAAdd to Basket

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MNAHTGTVRG KERYRSGTME YARMGYWEPD YVPKDTDVIA LFRVTPQEGV    50
DPIEASAAVA GESSTATWTV VWTDRLTAAE KYRAKCYRVD PVPGTPGSYF 100
AYIAYDLDLF EPGSIANLSA SIIGNVFGFK PLKALRLEDM RFPVAYVKTF 150
QGPATGIVVE RERLDKFGRP LLGATVKPKL GLSGRNYGRV VYEALKGGLD 200
FTKDDENINS QPFMHWRDRF LYCMEAVNRA QAASGEVKGT YLNVTAGTME 250
DMYERAEFAK ELGSVIVMID LVIGYTAIQS MAKWARRNDM ILHLHRAGHS 300
TYTRQKSHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDVC 350
REDFNPTMLE HGLFFDQSWA SLNKMMPVAS GGIHAGQMHQ LLNLLGEDVV 400
LQFGGGTIGH PMGIAAGAIA NRVALEAMIL ARNEGRDYVH EGPEILARAA 450
ETCTPLKAAL EVWKDVSFNY QSTDTPDFVP TALETV 486
Length:486
Mass (Da):53,788
Last modified:June 13, 2012 - v1
Checksum:i8DAB7860807EEB91
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP012279 Genomic DNA. Translation: BAL78590.1.
RefSeqiWP_015687864.1. NC_017082.1.
YP_005452702.1. NC_017082.1.

Genome annotation databases

EnsemblBacteriaiBAL78590; BAL78590; S23_53970.
GeneIDi12040411.
KEGGibrs:S23_53970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP012279 Genomic DNA. Translation: BAL78590.1 .
RefSeqi WP_015687864.1. NC_017082.1.
YP_005452702.1. NC_017082.1.

3D structure databases

ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAL78590 ; BAL78590 ; S23_53970 .
GeneIDi 12040411.
KEGGi brs:S23_53970.

Phylogenomic databases

KOi K01601.

Enzyme and pathway databases

BioCyci BSP335659:GL9K-5394-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 [LARGE SCALE GENOMIC DNA].
    Strain: S23321Imported.

Entry informationi

Entry nameiI0GCV3_9BRAD
AccessioniPrimary (citable) accession number: I0GCV3
Entry historyi
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: September 3, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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" By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi