Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P56648 (RBL_VITVI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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
OrganismVitis vinifera (Grape) [Reference proteome]
Taxonomic identifier29760 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsVitalesVitaceaeVitis

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Propeptide1 – 22 By similarity
PRO_0000031443
Chain3 – 475473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000031444

Sites

Active site1751Proton acceptor By similarity
Active site2941Proton acceptor By similarity
Metal binding2011Magnesium; via carbamate group By similarity
Metal binding2031Magnesium By similarity
Metal binding2041Magnesium By similarity
Binding site1231Substrate; in homodimeric partner By similarity
Binding site1731Substrate By similarity
Binding site1771Substrate By similarity
Binding site2951Substrate By similarity
Binding site3271Substrate By similarity
Binding site3791Substrate By similarity
Site3341Transition state stabilizer By similarity

Amino acid modifications

Modified residue31N-acetylproline By similarity
Modified residue141N6,N6,N6-trimethyllysine By similarity
Modified residue2011N6-carboxylysine By similarity
Disulfide bond247Interchain; in linked form By similarity

Experimental info

Sequence conflict321K → N Ref.1
Sequence conflict1271F → V Ref.1
Sequence conflict154 – 1552GI → RS Ref.1
Sequence conflict1701L → I Ref.1
Sequence conflict2261F → L Ref.1
Sequence conflict397 – 3982DS → EF Ref.1
Sequence conflict412 – 4143GNA → ETK Ref.1

Sequences

Sequence LengthMass (Da)Tools
P56648 [UniParc].

Last modified September 19, 2006. Version 2.
Checksum: EF561118F2BE2B00

FASTA47552,519
        10         20         30         40         50         60 
MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKPTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEESQFIAY VAYPLDLFEE GSVTNMFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL 

       250        260        270        280        290        300 
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDFVEKDRSR 

       370        380        390        400        410        420 
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNEIIRAASK WSPELAAACE VWKEIKFEFP AMDTL 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the chloroplast rbcL gene from grape (Vitis vinifera)."
Huang Y., Ma C., Li C.L., Wu N.H.
Acta Bot. Sin. 36:444-451(1994)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Phylogenetic analyses of Vitis (Vitaceae) based on complete chloroplast genome sequences: effects of taxon sampling and phylogenetic methods on resolving relationships among rosids."
Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J., Alverson A.J., Daniell H.
BMC Evol. Biol. 6:32-32(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Maxxa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ424856 Genomic DNA. Translation: ABE47542.1.
PIRA30610.
RefSeqYP_567084.1. NC_007957.1.

3D structure databases

ProteinModelPortalP56648.
SMRP56648. Positions 18-473.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4025045.
KEGGvvi:4025045.

Phylogenomic databases

eggNOGCOG1850.
KOK01601.

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_VITVI
AccessionPrimary (citable) accession number: P56648
Secondary accession number(s): Q0ZJ12
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 19, 2006
Last modified: May 14, 2014
This is version 84 of the entry and version 2 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