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K9PU29 (K9PU29_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:Lepto7376_0178 EMBL AFY36623.1
OrganismLeptolyngbya sp. PCC 7376 [Complete proteome] EMBL AFY36623.1
Taxonomic identifier111781 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesLeptolyngbya

Protein attributes

Sequence length471 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 site1711Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2901Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1971Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1991Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2001Magnesium By similarity HAMAP-Rule MF_01338
Binding site1191Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1691Substrate By similarity HAMAP-Rule MF_01338
Binding site1731Substrate By similarity HAMAP-Rule MF_01338
Binding site2911Substrate By similarity HAMAP-Rule MF_01338
Binding site3231Substrate By similarity HAMAP-Rule MF_01338
Binding site3751Substrate By similarity HAMAP-Rule MF_01338
Site3301Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1971N6-carboxylysine By similarity HAMAP-Rule MF_01338
Disulfide bond243Interchain; in linked form By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
K9PU29 [UniParc].

Last modified March 6, 2013. Version 1.
Checksum: C9C386CD54825A21

FASTA47152,214
        10         20         30         40         50         60 
MVQTKSAGFK AGVQDYRLTY YTPDYTPKDT DLLACFRMTP QAGVPAEECA AAVAAESSTG 

        70         80         90        100        110        120 
TWTTVWTDGL TDLDRYKGRC YHVEPVAGED NQYFCFVAYP LDLFEEGSIT NVLTSLVGNV 

       130        140        150        160        170        180 
FGFKALRALR LEDIRFPVAF IKTCPGNPHG ITVERDLLNK YGRPLLGCTI KPKLGLSAKN 

       190        200        210        220        230        240 
YGRAVYECLR GGLDFTKDDE NINSQPFMRW RDRFLFVQEA IEKAQAETNE VKGHYLNVTA 

       250        260        270        280        290        300 
ATCEEMIERA EFAKEIGTPI VMHDFITGGF TANTSLSKWC RKNGLLLHIH RAMHAVIDRQ 

       310        320        330        340        350        360 
KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGDRQGTLG FVDLMREDYV EEDRSRGVFF 

       370        380        390        400        410        420 
TQDWASAPGT MPVASGGIHV WHMPALVDIF GDDSCLQFGG GTLGHPWGNA PGATANRVAL 

       430        440        450        460        470 
EACVQARNEG RSLAREGNDV LREAGKWSPE LAAALNLWKE IKFEFDTVDT L 

« Hide

References

[1]"Finished genome of Leptolyngbya sp. PCC 7376."
US DOE Joint Genome Institute
Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N., Mikhailova N. expand/collapse author list , Pagani I., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.
Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003946 Genomic DNA. Translation: AFY36623.1.
RefSeqYP_007069457.1. NC_019683.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFY36623; AFY36623; Lepto7376_0178.
GeneID14086091.
KEGGlep:Lepto7376_0178.

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 nameK9PU29_9CYAN
AccessionPrimary (citable) accession number: K9PU29
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)