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P92397 (RBL_LUPAL) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismLupinus albus (White lupin) (Lupinus termis)
Taxonomic identifier3870 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Genisteae › Lupinus

Protein attributes

Sequence length455 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

Plastid › chloroplast 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›455›455Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062508

Sites

Active site1661Proton acceptor By similarity
Active site2851Proton acceptor By similarity
Metal binding1921Magnesium; via carbamate group By similarity
Metal binding1941Magnesium By similarity
Metal binding1951Magnesium By similarity
Binding site1141Substrate; in homodimeric partner By similarity
Binding site1641Substrate By similarity
Binding site1681Substrate By similarity
Binding site2861Substrate By similarity
Binding site3181Substrate By similarity
Binding site3701Substrate By similarity
Site3251Transition state stabilizer By similarity

Amino acid modifications

Modified residue51N6,N6,N6-trimethyllysine By similarity
Modified residue1921N6-carboxylysine By similarity
Disulfide bond238Interchain; in linked form By similarity

Experimental info

Non-terminal residue11
Non-terminal residue4551

Sequences

Sequence LengthMass (Da)Tools
P92397 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: FC9AD8CF670CE339

FASTA45550,315
        10         20         30         40         50         60 
SVGFKAGVKD YKLTYYTPDY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV 

        70         80         90        100        110        120 
WTDGLTSLDR YKGRCYHIEP VAGEENQFIA YVAYPLDLFE EGSVTNMFTS IVGNVFGFKA 

       130        140        150        160        170        180 
LRALRLEDLR IPNAYVKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV 

       190        200        210        220        230        240 
YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FCAEALYKAQ AETGEIKGHY LNATAGTCEE 

       250        260        270        280        290        300 
MIKRAVFARE LGVPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM 

       310        320        330        340        350        360 
HFRVLAKALR LSGGDHIHSG TVVGKLEGER EITLGFVDLL RDDFVEKDRS RGIYFTQDWV 

       370        380        390        400        410        420 
SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH PWGNAPGAVA NRVALEACVQ 

       430        440        450 
ARNEGRDLAS EGNQIIREAS KWSPELAAAC EVWKE

« Hide

References

[1]"Molecular phylogeny of the Papilionoideae (family Leguminosae): rbcL sequences versus chemical taxonomy."
Kaess E., Wink M.
Bot. Acta 108:149-162(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z70068 Genomic DNA. Translation: CAA93927.1.

3D structure databases

ProteinModelPortalP92397.
SMRP92397. Positions 9-455.
ModBaseSearch...

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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL_LUPAL
AccessionPrimary (citable) accession number: P92397
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: March 6, 2013
This is version 69 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

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