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F8BQM8 (F8BQM8_OLICM) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 22. 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 AEI04493.1
Ordered Locus Names:OCA4_pHCG3B00470 EMBL AEI04493.1
Encoded onPlasmid pHCG3B Ref.1 EMBL AEI04493.1
OrganismOligotropha carboxidovorans (strain OM4) [Complete proteome] [HAMAP] EMBL AEI04493.1
Taxonomic identifier1031710 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeOligotropha

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
F8BQM8 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: B200320194573F67

FASTA48653,763
        10         20         30         40         50         60 
MNDQSMTIRG KDRYKSGVMA YKKMGYWEPD YVPKDTDVIA LFRVTPQDGV DPIEAAAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTAAE KYRAKCYRVD PVPNSPGQYF AYIAYDLDLF EPGSISNLTA 

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

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

       250        260        270        280        290        300 
YLNVTAATME DMYERAEFAK ELGSCIVMID LVIGYTAIQS MAKWARKNDM ILHLHRAGHS 

       310        320        330        340        350        360 
TYTRQKNHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDIC REEFNPTKLE 

       370        380        390        400        410        420 
HGIFFDQNWA SLNKMMPVAS GGIHAGQMHQ LLDLLGEDVV LQFGGGTIGH PMGIQAGAIA 

       430        440        450        460        470        480 
NRVALEAMIL ARNEGRDYVA EGPEILAKAA ATCTPLKSAL EVWKDVTFNY ESTDAPDFVP 


TAIAAV 

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References

[1]"Complete Genome Sequences of the Chemolithoautotrophic Oligotropha carboxidovorans Strains OM4 and OM5."
Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., Meyer O.
J. Bacteriol. 193:5043-5043(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OM4 EMBL AEI04493.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002822 Genomic DNA. Translation: AEI04493.1.
RefSeqYP_005945987.1. NC_017536.1.

3D structure databases

ProteinModelPortalF8BQM8.
SMRF8BQM8. Positions 13-479.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEI04493; AEI04493; OCA4_pHCG3B00470.
GeneID12536746.
KEGGoco:OCA4_pHCG3B00470.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycOCAR1031710:GLI1-3562-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 nameF8BQM8_OLICM
AccessionPrimary (citable) accession number: F8BQM8
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: July 9, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)