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F8GNE1 (F8GNE1_CUPNN) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 19. Feed History...

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

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 AEI80316.1
Ordered Locus Names:CNE_2c13530 EMBL AEI80316.1
OrganismCupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1) (Ralstonia eutropha) [Complete proteome] [HAMAP] EMBL AEI80316.1
Taxonomic identifier1042878 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

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 site1781Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2961Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2041Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2061Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2071Magnesium By similarity HAMAP-Rule MF_01338
Binding site1261Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1761Substrate By similarity HAMAP-Rule MF_01338
Binding site1801Substrate By similarity HAMAP-Rule MF_01338
Binding site2971Substrate By similarity HAMAP-Rule MF_01338
Binding site3291Substrate By similarity HAMAP-Rule MF_01338
Binding site3811Substrate By similarity HAMAP-Rule MF_01338
Site3361Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2041N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F8GNE1 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 315108F9B1EC21CB

FASTA48653,777
        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 VILHLHRAGH 

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

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

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


PTASVA 

« Hide

References

[1]"Complete Genome Sequence of the Type Strain Cupriavidus necator N-1."
Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.
J. Bacteriol. 193:5017-5017(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43291 / DSM 13513 / N-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002878 Genomic DNA. Translation: AEI80316.1.
RefSeqYP_004681548.1. NC_015723.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEI80316; AEI80316; CNE_2c13530.
GeneID10921831.
KEGGcnc:CNE_2c13530.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycCNEC1042878:GH0Z-5042-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 nameF8GNE1_CUPNN
AccessionPrimary (citable) accession number: F8GNE1
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)