Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9ZI34 (RBL_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Ordered Locus Names:blr2585
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. 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.

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.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

The CO2/O2 specificity factor (tau) is 75.

KM=55 µM for ribulose 1,5-bisphosphate Ref.1

KM=66 µM for CO2

Vmax=2.8 µmol/min/mg enzyme with CO2 as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062620

Sites

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

Amino acid modifications

Modified residue2031N6-carboxylysine By similarity

Experimental info

Sequence conflict871H → Y in AAN61148. Ref.1
Sequence conflict871H → Y in BAC47850. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9ZI34 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4E949E13F57FDCE7

FASTA48653,818
        10         20         30         40         50         60 
MNAHTGTVRG KERYRSGVME YKRMGYWEPD YTPKDTDVIA LFRVTPQEGV DPIEASAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTAAE KYRAKCHRVD 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 LYCIEAVNRA QAASGEVKGT 

       250        260        270        280        290        300 
YLNITAGTME DMYERAEFAK ELGSCIVMID LVIGYTAIQS MAKWARRNDM ILHLHRAGHS 

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

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

       430        440        450        460        470        480 
NRVALEAMIL ARNEGRDYVH EGPEILAKAA QTCTPLKSAL EVWKDVTFNY QSTDTPDFVP 


TALETV 

« Hide

References

« Hide 'large scale' references
[1]"Closely related form I ribulose bisphosphate carboxylase/oxygenase molecules that possess different CO2/O2 substrate specificities."
Horken K.M., Tabita F.R.
Arch. Biochem. Biophys. 361:183-194(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], KINETIC PARAMETERS.
Strain: BJ110.
[2]"The Bradyrhizobium japonicum cbb locus."
Fischer H.-M., Bauer E., Hennecke H.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041820 Genomic DNA. Translation: AAD05386.1.
AY150332 Genomic DNA. Translation: AAN61148.1.
BA000040 Genomic DNA. Translation: BAC47850.1.
RefSeqNP_769225.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ9ZI34.
SMRQ9ZI34. Positions 13-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.blr2585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC47850; BAC47850; BAC47850.
GeneID1049510.
KEGGbja:blr2585.
PATRIC21188584. VBIBraJap65052_2551.

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-2608-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 nameRBL_BRADU
AccessionPrimary (citable) accession number: Q9ZI34
Secondary accession number(s): Q79UA8, Q8GKR7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families