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K9W672 (K9W672_9CYAN) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 9. 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:Cri9333_4173 EMBL AFZ14965.1
OrganismCrinalium epipsammum PCC 9333 [Complete proteome] EMBL AFZ14965.1
Taxonomic identifier1173022 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesCrinalium

Protein attributes

Sequence length476 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 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
K9W672 [UniParc].

Last modified March 6, 2013. Version 1.
Checksum: A35A0D4ED351FCFE

FASTA47653,156
        10         20         30         40         50         60 
MAYSQTKTQS KTGYKAGVQD YRLTYYTPDY TPKDTDVLAA FRVTPQPGVP PEEAGAAVAA 

        70         80         90        100        110        120 
ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA YIAYPLDLFE EGSVTNLLTS 

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

       190        200        210        220        230        240 
LSAKNYGRAV YEVLRGGLDF TKDDENINSQ PFMRWRDRFL FVQEAIEKAQ AETGEIKGHY 

       250        260        270        280        290        300 
LNVTAPTCEE MMERAEFAKE IGTPIIMHDY LTGGFTANTT LAKWCRRNGV LLHIHRAMHA 

       310        320        330        340        350        360 
VIDRQKNHGI HFRVLAKCLR MSGGDHLHSG TVVGKLEGEK GITMGFVDLM RENYVEQDRD 

       370        380        390        400        410        420 
RGIFFTQDWA SMPGVMPVAS GGIHVWHMPA LVEIFGDDSC LQFGGGTLGH PWGNAPGATA 

       430        440        450        460        470 
NRVALEACVQ ARNEGRNLMR EGGDVIREAC KWSPELAVAC ELWKEIKFEF EAMDTL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003620 Genomic DNA. Translation: AFZ14965.1.
RefSeqYP_007144475.1. NC_019753.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFZ14965; AFZ14965; Cri9333_4173.
GeneID14170772.
KEGGcep:Cri9333_4173.

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 nameK9W672_9CYAN
AccessionPrimary (citable) accession number: K9W672
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: February 19, 2014
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)