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Q0K1E0 (RBL1C_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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, chromosomal

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL1
Synonyms:cbbL, cbxLC, cfxLC
Ordered Locus Names:H16_B1395
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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.

Induction

Total RuBisCO activity (both chromosome and plasmid-derived enzyme) is high under lithoautotrophic growth conditions, intermediate when grown on fructose and poor when grown on pyruvate. HAMAP-Rule MF_01338

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" 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 – 486486Ribulose bisphosphate carboxylase large chain, chromosomal HAMAP-Rule MF_01338
PRO_0000273254

Sites

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

Amino acid modifications

Modified residue2041N6-carboxylysine By similarity

Experimental info

Sequence conflict83 – 886YRAKAY → SVQGL in AAA83745. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q0K1E0 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 47C20867581EDDB4

FASTA48653,729
        10         20         30         40         50         60 
MNAPESVQAK PRKRYDAGVM KYKEMGYWDG DYEPKDTDLL 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 KSLGSVIIMI DLIVGWTCIQ SMSNWCRQND MILHLHRAGH 

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

       370        380        390        400        410        420 
SRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLISLFGDDV VLQFGGGTIG HPQGIQAGAT 

       430        440        450        460        470        480 
ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCGPLRAA LDTWGDISFN YTPTDTSDFA 


PTASVA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the duplicate ribulose-1,5-bisphosphate carboxylase genes and cbb promoters of Alcaligenes eutrophus."
Kusian B., Bednarski R., Husemann M., Bowien B.
J. Bacteriol. 177:4442-4450(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION UNDER DIFFERENT GROWTH CONDITIONS.
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
[3]"Identification of cfxR, an activator gene of autotrophic CO2 fixation in Alcaligenes eutrophus."
Windhoevel U., Bowien B.
Mol. Microbiol. 5:2695-2705(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20584 Genomic DNA. Translation: AAA83745.1.
AM260480 Genomic DNA. Translation: CAJ96184.1.
M65065 Genomic DNA. Translation: AAA21981.1.
PIRI39557.
RefSeqYP_840914.1. NC_008314.1.

3D structure databases

ProteinModelPortalQ0K1E0.
SMRQ0K1E0. Positions 24-467.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_B1395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ96184; CAJ96184; H16_B1395.
GeneID4456354.
KEGGreh:H16_B1395.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMACTPLKQA.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-5100-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 nameRBL1C_CUPNH
AccessionPrimary (citable) accession number: Q0K1E0
Secondary accession number(s): P09657, P77811
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 52 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