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K9V3K1 (K9V3K1_9CYAN) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:rbcL HAMAP-Rule MF_01338
ORF Names:Cal6303_3045 EMBL AFZ01992.1
OrganismCalothrix sp. PCC 6303 [Complete proteome] EMBL AFZ01992.1
Taxonomic identifier1170562 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesRivulariaceaeCalothrix

Protein attributes

Sequence length476 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 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. HAMAP-Rule MF_01338

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. 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 site1761Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2951Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2021Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2041Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2051Magnesium By similarity HAMAP-Rule MF_01338
Binding site1241Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1741Substrate By similarity HAMAP-Rule MF_01338
Binding site1781Substrate By similarity HAMAP-Rule MF_01338
Binding site2961Substrate By similarity HAMAP-Rule MF_01338
Binding site3281Substrate By similarity HAMAP-Rule MF_01338
Binding site3801Substrate By similarity HAMAP-Rule MF_01338
Site3351Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2021N6-carboxylysine By similarity HAMAP-Rule MF_01338
Disulfide bond248Interchain; in linked form By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
K9V3K1 [UniParc].

Last modified March 6, 2013. Version 1.
Checksum: 376098CBB4F938A1

FASTA47653,127
        10         20         30         40         50         60 
MSYAQTKTQA KSGYQAGVKD YRLTYYTPDY TPKDTDILAA FRMTPQPGVP PEEAGAAVAA 

        70         80         90        100        110        120 
ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VAGEDNQYIA YIAYPLDLFE EGSVTNMLTS 

       130        140        150        160        170        180 
IVGNVFGFKA LRALRLEDLR IPVAYLKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG 

       190        200        210        220        230        240 
LSAKNYGRAV YECLRGGLDF TKDDENINSQ PFQRWRDRFL FVAEAIKKAQ AETGEIKGHY 

       250        260        270        280        290        300 
LNVTAPTCEE MMKRAEFAKE LEMPIVMHDY LTAGFTANTT LAHWCRDNGI LLHIHRAMHA 

       310        320        330        340        350        360 
VIDRQKNHGI HFRVLAKTLR MSGGDHIHTG TVVGKLEGEK GITMGFVDLL RENYVEQDKS 

       370        380        390        400        410        420 
RGIYFTQDWA SMPGVMAVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH PWGNAPGATA 

       430        440        450        460        470 
NRVALEACIQ ARNEGRNLAR EGNDVIREAC KWSPELAVAC ELWKEIKFEF EAMDTV 

« Hide

References

[1]"Finished chromosome of genome of Calothrix sp. PCC 6303."
Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A. expand/collapse author list , Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.
Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: PCC 6303 EMBL AFZ01992.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003610 Genomic DNA. Translation: AFZ01992.1.
RefSeqYP_007137964.1. NC_019751.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFZ01992; AFZ01992; Cal6303_3045.
GeneID14164484.
KEGGcalt:Cal6303_3045.

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 nameK9V3K1_9CYAN
AccessionPrimary (citable) accession number: K9V3K1
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: July 9, 2014
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)