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Q33015 (RBL_PTEVI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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
OrganismPteris vittata (Chinese ladder brake)
Taxonomic identifier13821 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaMoniliformopsesPolypodiopsidacore leptosporangiate fernsPolypodialesPteridaceaePteris

Protein attributes

Sequence length440 AA.
Sequence statusFragment.
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

Chain‹1 – ›440›440Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062577

Sites

Active site1651Proton acceptor By similarity
Active site2841Proton acceptor By similarity
Metal binding1911Magnesium; via carbamate group By similarity
Metal binding1931Magnesium By similarity
Metal binding1941Magnesium By similarity
Binding site1131Substrate; in homodimeric partner By similarity
Binding site1631Substrate By similarity
Binding site1671Substrate By similarity
Binding site2851Substrate By similarity
Binding site3171Substrate By similarity
Binding site3691Substrate By similarity
Site3241Transition state stabilizer By similarity

Amino acid modifications

Modified residue41N6,N6,N6-trimethyllysine By similarity
Modified residue1911N6-carboxylysine By similarity
Disulfide bond237Interchain; in linked form By similarity

Experimental info

Non-terminal residue11
Non-terminal residue4401

Sequences

Sequence LengthMass (Da)Tools
Q33015 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 904A064E8BB40578

FASTA44048,575
        10         20         30         40         50         60 
VGFKAGVKDY RLTYYTPEYK TKDTDILAAF RMTPQPGVPA EEAGAAVAAE SSTGTWTTVW 

        70         80         90        100        110        120 
TDGLTSLDRY KGRCYDIEPV AGEENQYIAY VAYPLDLFEE GSVTNMLTSI VGNVFGXKAX 

       130        140        150        160        170        180 
RALRLEDLRI LPAYSKTFIG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL CAKNYGRAVY 

       190        200        210        220        230        240 
ECLRGGLDFT KDDENVNSQP SMRWRDRFLF VAEALFKAQA ETGEVKGHYL NATAGTCEEM 

       250        260        270        280        290        300 
IKRATFAREL GAPIVMHDYL TGGFTANTSL AFYCRDNGLL LHIHRAMHAV IDRQRNHGMH 

       310        320        330        340        350        360 
LRVLAKALRM SGGDHIHAGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR GIYFTQDWVS 

       370        380        390        400        410        420 
MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA 

       430        440 
RNEGRDLARE GNEIIREASK 

« Hide

References

[1]"Phylogenetic relationships of dennstaedtioid ferns: evidence from rbcL sequences."
Wolf P.G., Soltis P.S., Soltis D.E.
Mol. Phylogenet. Evol. 3:383-392(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05941 Genomic DNA. Translation: AAC48966.1.

3D structure databases

ProteinModelPortalQ33015.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ33015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PTEVI
AccessionPrimary (citable) accession number: Q33015
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 72 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