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P34915 (RBL_PHYPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 92. 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
OrganismPhyscomitrella patens subsp. patens (Moss) [Reference proteome]
Taxonomic identifier3218 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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_0000031347
Chain3 – 475473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000031348

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 conflict91A → T in CAA52269. Ref.1
Sequence conflict301Q → H in CAA52269. Ref.1
Sequence conflict501A → L in CAA52269. Ref.1
Sequence conflict1901Y → N in CAA52269. Ref.1
Sequence conflict2511I → L in CAA52269. Ref.1
Sequence conflict255 – 2562QF → PC in CAA52269. Ref.1
Sequence conflict3011L → V in CAA52269. Ref.1
Sequence conflict3391R → L in CAA52269. Ref.1
Sequence conflict372 – 3743PGV → QVF in CAA52269. Ref.1
Sequence conflict3851W → G in CAA52269. Ref.1
Sequence conflict4141A → T in CAA52269. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P34915 [UniParc].

Last modified November 7, 2003. Version 2.
Checksum: 30A91B8A714507AF

FASTA47552,705
        10         20         30         40         50         60 
MSPRPEIKAG VGFKAGVKDY RLTYYTPDYQ TKDTDILAAF RMTPQPGVPA EECGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYAIEPV AGEENQYIAY VAYPLDLFEE GSVTNLFTSI 

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

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

       250        260        270        280        290        300 
NATAGTCEEM IKRAQFAREL GMPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
LDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERQ VTLGFVDLLR DDYIEKDRSR 

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

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFD TVDTL 

« Hide

References

« Hide 'large scale' references
[1]"An open reading frame (ycf11) is evolutionary conserved from Cyanobacteria to the plastid DNAs of Archegoniates and Gymnosperms is modified in the plastid DNAs of Dicots and is not plastome encoded in Monocots."
Kruse S., Martin W., Wehe M., Reski R.
J. Plant Physiol. 146:258-262(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Physcomitrella patens chloroplast genes."
Sugita M., Sugiura C.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Protonema.
[3]"Complete chloroplast DNA sequence of the moss Physcomitrella patens: evidence for the loss and relocation of rpoA from the chloroplast to the nucleus."
Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.
Nucleic Acids Res. 31:5324-5331(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Gransden 2004.
[4]"Cytokinin affects nuclear- and plastome-encoded energy-converting plastid enzymes."
Kasten B., Buck F., Nuske J., Reski R.
Planta 201:261-272(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 184-195.
Tissue: Protonema.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74156 Genomic DNA. Translation: CAA52269.1.
AB066207 Genomic DNA. Translation: BAB62086.1.
AP005672 Genomic DNA. Translation: BAC85044.1.
PIRS34663.
RefSeqNP_904194.1. NC_005087.1.

3D structure databases

ProteinModelPortalP34915.
SMRP34915. Positions 18-473.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP34915.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2546763.
KEGGppp:PhpapaCp031.

Phylogenomic databases

KOK01601.
ProtClustDBCHL00040.

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_PHYPA
AccessionPrimary (citable) accession number: P34915
Secondary accession number(s): Q95FY7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 7, 2003
Last modified: February 19, 2014
This is version 92 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