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P48699 (RBL_DENCL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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
OrganismDendrophthora clavata (Columbian mistletoe)
Taxonomic identifier3965 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeDendrophthora

Protein attributes

Sequence length474 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 – 474›474Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062439

Sites

Active site1741Proton acceptor By similarity
Active site2931Proton acceptor By similarity
Metal binding2001Magnesium; via carbamate group By similarity
Metal binding2021Magnesium By similarity
Metal binding2031Magnesium By similarity
Binding site1221Substrate; in homodimeric partner By similarity
Binding site1721Substrate By similarity
Binding site1761Substrate By similarity
Binding site2941Substrate By similarity
Binding site3261Substrate By similarity
Binding site3781Substrate By similarity
Site3331Transition state stabilizer By similarity

Amino acid modifications

Modified residue131N6,N6,N6-trimethyllysine By similarity
Modified residue2001N6-carboxylysine By similarity
Disulfide bond246Interchain; in linked form By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P48699 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 6E9F94ED90BBDFF3

FASTA47452,452
        10         20         30         40         50         60 
SPQXETKASV GFKAGVKDYK LTYYTPDYKT KDTDILAAFR VTPQPGVPPE EAGAAVAAES 

        70         80         90        100        110        120 
STGTWTTVWT DGLTSLDRYK GRCYHIEPVA GEENHFIAYV AYPLDLFEEG SVTNMFTSIV 

       130        140        150        160        170        180 
GNVFGFKALR ALRLEDLRIP PAYSKTFQGP PHGIQVERDK LNKYGRPLLG CTIKPKLGLS 

       190        200        210        220        230        240 
AKNYGRAVYE CLRGGLDFTK DDENVNSQPF MRWRDRFVFC AEAIYKAQAE TGEIKGHYLN 

       250        260        270        280        290        300 
ATAGTCEEMI KRAVFARELG VPIIMHDYLT GGFTANTSLA HYCRDNGLLL HIHRAMHAVI 

       310        320        330        340        350        360 
DRQKNHGIHF RVLAKALRMS GGDHIHSGTV VGKLEGERDI TLGFVDLLRD DFIAKDRSRG 

       370        380        390        400        410        420 
IYFTQDWVSL PGVLPVASGG IHVWHMPALT EIFGDDSVLQ FGGGTLGHPW GNAPGAVANR 

       430        440        450        460        470 
VALEACVQAR NEGRDLAREG NEIIREASKW SPELAAACEV WKEIKFEFQA VDTL 

« Hide

References

[1]"A comparision of angiosperm phylogenies from nuclear 18S rRNA and rbcL sequences."
Nickrent D.L., Soltis D.E.
Ann. Mo. Bot. Gard. 82:208-234(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26069 Genomic DNA. Translation: AAB97296.1.

3D structure databases

ProteinModelPortalP48699.
SMRP48699. Positions 17-472.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP48699.

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_DENCL
AccessionPrimary (citable) accession number: P48699
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 68 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