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I0GCV3 (I0GCV3_9BRAD) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL HAMAP-Rule MF_01338 EMBL BAL78590.1
ORF Names:S23_53970 EMBL BAL78590.1
OrganismBradyrhizobium sp. S23321 [Complete proteome] EMBL BAL78590.1
Taxonomic identifier335659 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity. HAMAP-Rule MF_01338

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. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1771Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2951Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2031Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2051Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2061Magnesium By similarity HAMAP-Rule MF_01338
Binding site1251Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1751Substrate By similarity HAMAP-Rule MF_01338
Binding site1791Substrate By similarity HAMAP-Rule MF_01338
Binding site2961Substrate By similarity HAMAP-Rule MF_01338
Binding site3281Substrate By similarity HAMAP-Rule MF_01338
Binding site3801Substrate By similarity HAMAP-Rule MF_01338
Site3351Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2031N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
I0GCV3 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 8DAB7860807EEB91

FASTA48653,788
        10         20         30         40         50         60 
MNAHTGTVRG KERYRSGTME YARMGYWEPD YVPKDTDVIA LFRVTPQEGV DPIEASAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTAAE KYRAKCYRVD PVPGTPGSYF AYIAYDLDLF EPGSIANLSA 

       130        140        150        160        170        180 
SIIGNVFGFK PLKALRLEDM RFPVAYVKTF QGPATGIVVE RERLDKFGRP LLGATVKPKL 

       190        200        210        220        230        240 
GLSGRNYGRV VYEALKGGLD FTKDDENINS QPFMHWRDRF LYCMEAVNRA QAASGEVKGT 

       250        260        270        280        290        300 
YLNVTAGTME DMYERAEFAK ELGSVIVMID LVIGYTAIQS MAKWARRNDM ILHLHRAGHS 

       310        320        330        340        350        360 
TYTRQKSHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDVC REDFNPTMLE 

       370        380        390        400        410        420 
HGLFFDQSWA SLNKMMPVAS GGIHAGQMHQ LLNLLGEDVV LQFGGGTIGH PMGIAAGAIA 

       430        440        450        460        470        480 
NRVALEAMIL ARNEGRDYVH EGPEILARAA ETCTPLKAAL EVWKDVSFNY QSTDTPDFVP 


TALETV 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012279 Genomic DNA. Translation: BAL78590.1.
RefSeqYP_005452702.1. NC_017082.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAL78590; BAL78590; S23_53970.
GeneID12040411.
KEGGbrs:S23_53970.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycBSP335659:GL9K-5394-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameI0GCV3_9BRAD
AccessionPrimary (citable) accession number: I0GCV3
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: June 11, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)