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L0GWD2 (L0GWD2_9GAMM) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 9. 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
ORF Names:Thimo_0765 EMBL AGA89604.1
OrganismThioflavicoccus mobilis 8321 [Complete proteome] EMBL AGA89604.1
Taxonomic identifier765912 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThioflavicoccus

Protein attributes

Sequence length472 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 site1671Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2861Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1931Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Binding site1151Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1651Substrate By similarity HAMAP-Rule MF_01338
Binding site1691Substrate By similarity HAMAP-Rule MF_01338
Binding site2871Substrate By similarity HAMAP-Rule MF_01338
Binding site3191Substrate By similarity HAMAP-Rule MF_01338
Binding site3711Substrate By similarity HAMAP-Rule MF_01338
Site3261Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
L0GWD2 [UniParc].

Last modified March 6, 2013. Version 1.
Checksum: 265A348FD4ADD3DF

FASTA47252,514
        10         20         30         40         50         60 
MAKTYNAGVK DYRETYWMPD YTPKDTDILA CFKITPQPGV PREEAAAAVA AESSTGTWTT 

        70         80         90        100        110        120 
VWTDLLTDLD YYKGRAYAIE DVPGDDERFY AFIAYPIDLF EEGSVVNVFT SLVGNVFGFK 

       130        140        150        160        170        180 
AVRTLRLEDV RFPIAYVMTC NGPPHGIQVE RDIMNKYGRP LLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENVNS QPFMRWRQRF DFVMEAIDKA ESETGERKGH YLNVTAPTPD 

       250        260        270        280        290        300 
EMFKRAEHAK ELGAPIIMHD YITGGWCANT GLAQWCRDNG VLLHIHRAMH AVIDRHPHHG 

       310        320        330        340        350        360 
IHFRVLAKLL RLSGGDHLHT GTVVGKLEGD RAATLGWIDL LRESYVEEDR SRGIFFDQDW 

       370        380        390        400        410        420 
GSMPGVFAVA SGGIHVWHMP ALVTIFGDDA VLQFGGGTLG HPWGNAAGAA ANRVALEACV 

       430        440        450        460        470 
EARNRGVAIE KEGKEVLTAA ANNSPELKAA METWKEIKFE FDTVDKLDVA HK 

« Hide

References

[1]"Complete sequence of chromosome of Thioflavicoccus mobilis 8321."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K. expand/collapse author list , Liu Z., Imhoff J., Thiel V., Frigaard N.-U., Bryant D., Woyke T.
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 8321 EMBL AGA89604.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003051 Genomic DNA. Translation: AGA89604.1.
RefSeqYP_007243234.1. NC_019940.1.

3D structure databases

ProteinModelPortalL0GWD2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAGA89604; AGA89604; Thimo_0765.
GeneID14303029.
KEGGtmb:Thimo_0765.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

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 nameL0GWD2_9GAMM
AccessionPrimary (citable) accession number: L0GWD2
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: June 11, 2014
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)