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P0C2C2 (RBL1C_CUPNE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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, chromosomal

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL1
Synonyms:cbbL, cbxLC, cfxLC
OrganismCupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha)
Taxonomic identifier106590 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

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.

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.

Post-translational modification

The disulfide bond which can form between Cys-278 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".

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Ribulose bisphosphate carboxylase large chain, chromosomal HAMAP-Rule MF_01338
PRO_0000062641

Sites

Active site1781Proton acceptor
Active site2961Proton acceptor
Metal binding2041Magnesium; via carbamate group
Metal binding2061Magnesium
Metal binding2071Magnesium
Binding site1261Substrate; in homodimeric partner
Binding site1761Substrate
Binding site1801Substrate
Binding site2971Substrate
Binding site3291Substrate
Binding site3811Substrate
Site3361Transition state stabilizer

Amino acid modifications

Modified residue2041N6-carboxylysine HAMAP-Rule MF_01338

Secondary structure

................................................................................. 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C2C2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 66EAB4A11982FAB5

FASTA48653,840
        10         20         30         40         50         60 
MNAPETIQAK PRKRYDAGVM KYKEMGYWDG DYVPKDTDVL ALFRITPQDG VDPVEAAAAV 

        70         80         90        100        110        120 
AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF FCYVAYDLSL FEEGSIANLT 

       130        140        150        160        170        180 
ASIIGNVFSF KPIKAARLED MRFPVAYVKT FAGPSTGIIV ERERLDKFGR PLLGATTKPK 

       190        200        210        220        230        240 
LGLSGRNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG 

       250        260        270        280        290        300 
SYLNVTAGTM EEMYRRAEFA KSLGSVIIMV DLIVGWTCIQ SMSNWCRQND MILHLHRAGH 

       310        320        330        340        350        360 
GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV CRDAYTQTDL 

       370        380        390        400        410        420 
TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV VLQFGGGTIG HPQGIQAGAT 

       430        440        450        460        470        480 
ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCAPLRAA LDTWGDITFN YTPTDTSDFV 


PTASVA 

« Hide

References

[1]"Sequence analysis of the Alcaligenes eutrophus chromosomally encoded ribulose bisphosphate carboxylase large and small subunit genes and their gene products."
Andersen K., Caton J.
J. Bacteriol. 169:4547-4558(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.
[2]Andersen K.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits."
Hansen S., Vollan V.B., Hough E., Andersen K.
J. Mol. Biol. 288:609-621(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17744 Genomic DNA. Translation: AAC28129.1.
PIRRKALLE. A26954.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXNX-ray2.70A/C/E/G1-486[»]
ProteinModelPortalP0C2C2.
SMRP0C2C2. Positions 24-467.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP0C2C2.

Entry information

Entry nameRBL1C_CUPNE
AccessionPrimary (citable) accession number: P0C2C2
Secondary accession number(s): P09657, P77811
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 39 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references