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Q31750 (RBL_CALCA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 67. 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
OrganismCalycophyllum candidissimum
Taxonomic identifier43450 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Rubiaceae › Ixoroideae › Condamineeae › Calycophyllum

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-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.

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 – 469›469Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062389

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

Sequences

Sequence LengthMass (Da)Tools
Q31750 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3D063EF0DE032F97

FASTA46951,944
        10         20         30         40         50         60 
SVGFKAGVKE YKLTYYTPEY ETKDTDILAA FRVTPQPGVP PEEAGXAVXX ESSTGTWTAV 

        70         80         90        100        110        120 
WTDGLTSLDR YKGRCYXIEP VPGEEDQYIA YVAYPLDXFE EGSVTNMFTS IVGNVFGFKA 

       130        140        150        160        170        180 
LXALRLEDLR IPPAYIKTFE GPPHGIQVER DKLNKYGRPL LXCTIKPKLG LSAKNYGRAC 

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

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

       310        320        330        340        350        360 
HFRVLAKALR MSGGDHIHSG TVVGKLEGER DITLGFVDLL RDDFIEKDRS RGIYFTQDWS 

       370        380        390        400        410        420 
SLPGVLPVXS GGIHVXHMPA LTEIFGDDSV XXFGGGTLGH PWGNAPGAVA NRVSLEACVK 

       430        440        450        460 
ARNEGRDLAA EGNEIIREAS KWSPELAAAC EVWKEIRFNF AAVDTLDPS

« Hide

References

[1]"Subfamilial and tribal relationships in the Rubiaceae based on rbcL sequence data."
Bremer B., Andreasen K., Olsson D.
Ann. Mo. Bot. Gard. 82:383-397(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X83627 Genomic DNA. Translation: CAA58606.1.

3D structure databases

ProteinModelPortalQ31750.
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_CALCA
AccessionPrimary (citable) accession number: Q31750
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: March 6, 2013
This is version 67 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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