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Q1ACK0 (RBL_CHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:rbcL
Encoded onPlastid; Chloroplast
OrganismChara vulgaris (Common stonewort)
Taxonomic identifier55564 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaCharophyceaeCharalesCharaceaeChara

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subcellular location

Plastidchloroplast 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.

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22 By similarity
PRO_0000251418
Chain3 – 475473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000251419

Sites

Active site1751Proton acceptor By similarity
Active site2941Proton acceptor By similarity
Metal binding2011Magnesium; via carbamate group By similarity
Metal binding2031Magnesium By similarity
Metal binding2041Magnesium By similarity
Binding site1231Substrate; in homodimeric partner By similarity
Binding site1731Substrate By similarity
Binding site1771Substrate By similarity
Binding site2951Substrate By similarity
Binding site3271Substrate By similarity
Binding site3791Substrate By similarity
Site3341Transition state stabilizer By similarity

Amino acid modifications

Modified residue31N-acetylproline By similarity
Modified residue141N6,N6,N6-trimethyllysine By similarity
Modified residue2011N6-carboxylysine By similarity
Disulfide bond247Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1ACK0 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: AD02CA001E110B06

FASTA47552,700
        10         20         30         40         50         60 
MSPQTETKTS AGFKAGVKDY RLTYYTPEYK TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV AGEENQFIAY VAYPLDLFEE GSVTNLFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEAIYKSQA ETGEIKGHYL 

       250        260        270        280        290        300 
NATAGTCEEM LKRAQCAREL GMPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
LDRQKNHGMH FRVLAKALRL SGGDHVHSGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR 

       370        380        390        400        410        420 
GVYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFE TIDTL 

« Hide

References

[1]"The chloroplast genome sequence of Chara vulgaris sheds new light into the closest green algal relatives of land plants."
Turmel M., Otis C., Lemieux C.
Mol. Biol. Evol. 23:1324-1338(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ229107 Genomic DNA. Translation: ABA61952.1.
RefSeqYP_635747.1. NC_008097.1.

3D structure databases

ProteinModelPortalQ1ACK0.
SMRQ1ACK0. Positions 10-463.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ1ACK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4100318.

Phylogenomic databases

ProtClustDBCHL00040.

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 nameRBL_CHAVU
AccessionPrimary (citable) accession number: Q1ACK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 11, 2006
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families