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M4ZEA6 (M4ZEA6_9BRAD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 9. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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
ORF Names:S58_58790 EMBL BAM91856.1
OrganismBradyrhizobium oligotrophicum S58 [Complete proteome] EMBL BAM91856.1
Taxonomic identifier1245469 [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
M4ZEA6 [UniParc].

Last modified May 29, 2013. Version 1.
Checksum: 82AD64B14C294039

FASTA48653,956
        10         20         30         40         50         60 
MNDQSITVRG KDRYKSGVME YKKMGYWEPS YQPKDTDVIA LFRVTPQDGV DPTEACAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTAAE KYRAKCYRVE PVPGSPGSYF AYIAYDLDLF EPGSISNLTA 

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

       190        200        210        220        230        240 
GLSGRNYGRV VYEALKGGLD FTKDDENINS QPFMHWRERF LYCMEAVNKA QAASGEIKGT 

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

       310        320        330        340        350        360 
TYTRQRSHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDIC REDFNPMRLE 

       370        380        390        400        410        420 
HGVFFDQNWA SLNKLMPVAS GGIHAGQMHQ LLDLLGEDVV LQFGGGTIGH PRGIAAGATA 

       430        440        450        460        470        480 
NRVALEAMIL ARNEGRDYVH EGPEILAKAA QTCTPLREAL EIWKDVTFNY ESTDSPDFVP 


TVTPAA 

« Hide

References

[1]"Genome Analysis Suggests that the Soil Oligotrophic Bacterium Agromonas oligotrophica (Bradyrhizobium oligotrophicum) Is a Nitrogen-Fixing Symbiont of Aeschynomene indica."
Okubo T., Fukushima S., Itakura M., Oshima K., Longtonglang A., Teaumroong N., Mitsui H., Hattori M., Hattori R., Hattori T., Minamisawa K.
Appl. Environ. Microbiol. 79:2542-2551(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: S58 EMBL BAM91856.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP012603 Genomic DNA. Translation: BAM91856.1.
RefSeqYP_007515443.1. NC_020453.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAM91856; BAM91856; S58_58790.
GeneID14686564.
KEGGaol:S58_58790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

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 nameM4ZEA6_9BRAD
AccessionPrimary (citable) accession number: M4ZEA6
Entry history
Integrated into UniProtKB/TrEMBL: May 29, 2013
Last sequence update: May 29, 2013
Last modified: February 19, 2014
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)