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Q07210 (RBL_COLPU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 65. 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
OrganismColeonema pulchellum (Confetti bush)
Taxonomic identifier23551 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Sapindales › Rutaceae › Coleonema

Protein attributes

Sequence length469 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 MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP 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 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 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 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 – 469›469Ribulose bisphosphate carboxylase large chain HAMAP MF_01338
PRO_0000062414

Sites

Active site1691Proton acceptor By similarity
Active site2881Proton acceptor By similarity
Metal binding1951Magnesium; via carbamate group By similarity
Metal binding1971Magnesium By similarity
Metal binding1981Magnesium By similarity
Binding site1171Substrate; in homodimeric partner By similarity
Binding site1671Substrate By similarity
Binding site1711Substrate By similarity
Binding site2891Substrate By similarity
Binding site3211Substrate By similarity
Binding site3731Substrate By similarity
Site3281Transition state stabilizer By similarity

Amino acid modifications

Modified residue81N6,N6,N6-trimethyllysine By similarity
Modified residue1951N6-carboxylysine By similarity
Disulfide bond241Interchain; in linked form By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q07210 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E39EC42D3A0B5C63

FASTA46951,995
        10         20         30         40         50         60 
TKASVGFKAG VKDYKLTYYT PDYVTKDTDI LAAFRVTPQP GVPPEEAGAA VAAESSTGTW 

        70         80         90        100        110        120 
TTVWTDGLTS LDRYKGRCYN IEPVAGEEHQ YICYVAYPLD LFEEGSVTNM FTSIVGNVFG 

       130        140        150        160        170        180 
FKALRALRLE DLRIPPAYSK TFQGPPHGIQ VERDKLNKYG RPLLGCTIKP KLGLSAKNYG 

       190        200        210        220        230        240 
RAVYECLRGG LDFTKDDENV NSQPFMRWRD RFLFCAERIY KSQAETGEIK GHYLNATAGT 

       250        260        270        280        290        300 
CEEMIKRAVF ARELGVPIVM HDYLTGGFTA NTSLAHYCRD NGLLLHIHRA MHAVIDRQKN 

       310        320        330        340        350        360 
HGIHFRVLAK ALRMSGGDHI HAGTVVGKLE GERDITLGFV DLLRDDFIEK DRSRGIYFTQ 

       370        380        390        400        410        420 
DWVSLPGVLP VASGGIHVWH MPALTEIFGD DSVLQFGGGT LGHPWGNAPG AVANRVALEA 

       430        440        450        460 
CVQARNEGRD LAREGNEIIR EASKWSPELA AACEVWKAIK FEFPAMDTL

« Hide

References

[1]"Affinities of the Australian endemic Akaniaceae: new evidence from rbcL sequences."
Gadek P.A., Quinn C.J., Rodman J.E., Karol K.G., Conti E., Price R.A., Fernando E.S.
Aust. Syst. Bot. 5:717-724(1992) [Agricola: IND93029186]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L12567 Genomic DNA. Translation: AAA33077.2.

3D structure databases

ProteinModelPortalQ07210.
SMRQ07210. Positions 12-467.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01338. RuBisCO_L_type1.
[Tree]
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
Gene3DG3DSA:3.20.20.110. RuBisCO_large. 1 hit.
G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
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_COLPU
AccessionPrimary (citable) accession number: Q07210
Secondary accession number(s): Q39564
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 28, 2011
This is version 65 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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