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Q7NIM7 (RBL_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. 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
Synonyms:rbcL
Ordered Locus Names:glr2156
OrganismGloeobacter violaceus (strain PCC 7421) [Reference proteome] [HAMAP]
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

Protein attributes

Sequence length474 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 in the photorespiration process. 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; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.

Post-translational modification

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover 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.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062623

Sites

Active site1741Proton acceptor By similarity
Active site2931Proton acceptor By similarity
Metal binding2001Magnesium; via carbamate group By similarity
Metal binding2021Magnesium By similarity
Metal binding2031Magnesium By similarity
Binding site1221Substrate; in homodimeric partner By similarity
Binding site1721Substrate By similarity
Binding site1761Substrate By similarity
Binding site2941Substrate By similarity
Binding site3261Substrate By similarity
Binding site3781Substrate By similarity
Site3331Transition state stabilizer By similarity

Amino acid modifications

Modified residue2001N6-carboxylysine By similarity
Disulfide bond246Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NIM7 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 6474FEF981055201

FASTA47452,855
        10         20         30         40         50         60 
MSYTKTQAKA GYQAGVKDYR LTYYTPDYTP KDTDVLAAFR VTPQPGVPIE EAGAAVAAES 

        70         80         90        100        110        120 
STGTWTTVWT DGLTELDRYK GRCYDIEPVP GEDNQWICYI AYPLDLFEEG SVTNVLTSLV 

       130        140        150        160        170        180 
GNVFGFKALR ALRLEDIRFP IALVKTYQGP PHGIVVERDK INKYGRPLLG CTIKPKLGLS 

       190        200        210        220        230        240 
AKNYGRAVYE CLRGGLDFTK DDENINSQPF MRWRDRFLFV QDAIVKSQAE TGEIKGHYLN 

       250        260        270        280        290        300 
CTAGTCEEMM ERAEFAKELK TPIIMHDYLT GGFTANTTLA KWCRRNGILL HIHRAMHAVI 

       310        320        330        340        350        360 
DRQKNHGIHF RVLAKCLRLS GGDHIHTGTV VGKLEGERAS TMGFVDLLRE EHVERDLSRG 

       370        380        390        400        410        420 
IYFTQDWASM PGVMAVASGG IHVWHMPALL DIFGDDAVLQ FGGGTLGHPW GNAPGATANR 

       430        440        450        460        470 
VALEACVKAR NEGRDLMREA GDIIREAARW SPELAAACEL WKEIKFEYEA VDKL 

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000045 Genomic DNA. Translation: BAC90097.1.
RefSeqNP_925102.1. NC_005125.1.

3D structure databases

ProteinModelPortalQ7NIM7.
SMRQ7NIM7. Positions 8-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING251221.gvip295.

Proteomic databases

PRIDEQ7NIM7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC90097; BAC90097; BAC90097.
GeneID2600557.
KEGGgvi:gvip295.
PATRIC22043775. VBIGloVio86258_2190.

Phylogenomic databases

eggNOGCOG1850.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.
PhylomeDBQ7NIM7.

Enzyme and pathway databases

BioCycGVIO251221:GH9A-2182-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_GLOVI
AccessionPrimary (citable) accession number: Q7NIM7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 75 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