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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

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".1 Publication

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

Cofactori

Mg2+2 PublicationsNote: Binds 1 Mg2+ ion per subunit.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei123Substrate; in homodimeric partner1
Binding sitei173Substrate1
Active sitei175Proton acceptor1
Binding sitei177Substrate1
Metal bindingi201Magnesium; via carbamate group2 Publications1
Metal bindingi203Magnesium2 Publications1
Metal bindingi204Magnesium2 Publications1
Active sitei294Proton acceptor1
Binding sitei295Substrate1
Binding sitei327Substrate1
Sitei334Transition state stabilizer1
Binding sitei379Substrate1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase, Monooxygenase, Oxidoreductase
Biological processCalvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis
LigandMagnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:rbcL
Encoded oniPlastid; Chloroplast
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
Proteomesi
  • UP000006906 Componenti: Chloroplast

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000311751 – 21 Publication2
ChainiPRO_00000311763 – 475Ribulose bisphosphate carboxylase large chainAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylproline1 Publication1
Modified residuei1044-hydroxyproline2 Publications1
Modified residuei1514-hydroxyproline2 Publications1
Modified residuei201N6-carboxylysine3 Publications1
Disulfide bondi247Interchain; in linked form2 Publications
Modified residuei256S-methylcysteine2 Publications1
Modified residuei369S-methylcysteine2 Publications1

Post-translational modificationi

The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bond reported in 1IR2 may be the result of oxidation during crystallization.By similarityCurated
The electron density found in the position of Thr-471 (PubMed:11866526 only) suggests it is either O-methylthreonine, or Ile, which may be produced by RNA editing.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Hydroxylation, Methylation

Proteomic databases

PaxDbiP00877
PRIDEiP00877

PTM databases

iPTMnetiP00877

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.2 Publications

Protein-protein interaction databases

STRINGi3055.DAA00950

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP00877
SMRiP00877
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00877

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IIVP Eukaryota
COG1850 LUCA
InParanoidiP00877
KOiK01601

Family and domain databases

CDDicd08212 RuBisCO_large_I, 1 hit
Gene3Di3.20.20.110, 1 hit
3.30.70.150, 1 hit
HAMAPiMF_01338 RuBisCO_L_type1, 1 hit
InterProiView protein in InterPro
IPR033966 RuBisCO
IPR020878 RuBisCo_large_chain_AS
IPR000685 RuBisCO_lsu_C
IPR036376 RuBisCO_lsu_C_sf
IPR017443 RuBisCO_lsu_fd_N
IPR036422 RuBisCO_lsu_N_sf
IPR020888 RuBisCO_lsuI
PANTHERiPTHR42704 PTHR42704, 1 hit
PfamiView protein in Pfam
PF00016 RuBisCO_large, 1 hit
PF02788 RuBisCO_large_N, 1 hit
SFLDiSFLDS00014 RuBisCO, 2 hits
SUPFAMiSSF51649 SSF51649, 1 hit
SSF54966 SSF54966, 1 hit
PROSITEiView protein in PROSITE
PS00157 RUBISCO_LARGE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00877-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVPQTETKAG AGFKAGVKDY RLTYYTPDYV VRDTDILAAF RMTPQLGVPP
60 70 80 90 100
EECGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV PGEDNQYIAY
110 120 130 140 150
VAYPIDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYVKTFVG
160 170 180 190 200
PPHGIQVERD KLNKYGRGLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFLF VAEAIYKAQA ETGEVKGHYL NATAGTCEEM
260 270 280 290 300
MKRAVCAKEL GVPIIMHDYL TGGFTANTSL AIYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQRNHGIH FRVLAKALRM SGGDHLHSGT VVGKLEGERE VTLGFVDLMR
360 370 380 390 400
DDYVEKDRSR GIYFTQDWCS MPGVMPVASG GIHVWHMPAL VEIFGDDACL
410 420 430 440 450
QFGGGTLGHP WGNAPGAAAN RVALEACTQA RNEGRDLARE GGDVIRSACK
460 470
WSPELAAACE VWKEIKFEFD TIDKL
Length:475
Mass (Da):52,543
Last modified:July 21, 1986 - v1
Checksum:i5A9BFD394CF7D4D4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti46L → P in strain: 137c and CC-503. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01399 Genomic DNA Translation: AAA84449.1
FJ423446 Genomic DNA Translation: ACJ50136.1
BK000554 Genomic DNA Translation: DAA00950.1
PIRiA01097 RKKML
RefSeqiNP_958405.1, NC_005353.1

Genome annotation databases

GeneIDi2717040
KEGGicre:ChreCp049

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01399 Genomic DNA Translation: AAA84449.1
FJ423446 Genomic DNA Translation: ACJ50136.1
BK000554 Genomic DNA Translation: DAA00950.1
PIRiA01097 RKKML
RefSeqiNP_958405.1, NC_005353.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GK8X-ray1.40A/C/E/G1-475[»]
1IR2X-ray1.84A/B/C/D/E/F/G/H/S/T/U/V/W/X/Y/Z1-475[»]
1UW9X-ray2.05A/B/E/H/K/O/R/V1-475[»]
1UWAX-ray2.30A/B/E/H/K/O/R/V1-475[»]
1UZDX-ray2.40A/B/E/H/K/O/R/V1-475[»]
1UZHX-ray2.20A/B/E/H/K/O/R/V1-475[»]
2V63X-ray1.80A/B/C/D/E/F/G/H1-475[»]
2V67X-ray2.00A/B/C/D/E/F/G/H1-475[»]
2V68X-ray2.30A/B/C/D/E/F/G/H1-475[»]
2V69X-ray2.80A/B/C/D/E/F/G/H1-475[»]
2V6AX-ray1.50A/B/C/D/E/F/G/H1-475[»]
2VDHX-ray2.30A/B/C/D/E/F/G/H1-475[»]
2VDIX-ray2.65A/B/C/D/E/F/G/H1-475[»]
5BS2X-ray1.97A/B462-473[»]
R462-467[»]
ProteinModelPortaliP00877
SMRiP00877
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.DAA00950

PTM databases

iPTMnetiP00877

Proteomic databases

PaxDbiP00877
PRIDEiP00877

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2717040
KEGGicre:ChreCp049

Phylogenomic databases

eggNOGiENOG410IIVP Eukaryota
COG1850 LUCA
InParanoidiP00877
KOiK01601

Miscellaneous databases

EvolutionaryTraceiP00877

Family and domain databases

CDDicd08212 RuBisCO_large_I, 1 hit
Gene3Di3.20.20.110, 1 hit
3.30.70.150, 1 hit
HAMAPiMF_01338 RuBisCO_L_type1, 1 hit
InterProiView protein in InterPro
IPR033966 RuBisCO
IPR020878 RuBisCo_large_chain_AS
IPR000685 RuBisCO_lsu_C
IPR036376 RuBisCO_lsu_C_sf
IPR017443 RuBisCO_lsu_fd_N
IPR036422 RuBisCO_lsu_N_sf
IPR020888 RuBisCO_lsuI
PANTHERiPTHR42704 PTHR42704, 1 hit
PfamiView protein in Pfam
PF00016 RuBisCO_large, 1 hit
PF02788 RuBisCO_large_N, 1 hit
SFLDiSFLDS00014 RuBisCO, 2 hits
SUPFAMiSSF51649 SSF51649, 1 hit
SSF54966 SSF54966, 1 hit
PROSITEiView protein in PROSITE
PS00157 RUBISCO_LARGE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRBL_CHLRE
AccessioniPrimary (citable) accession number: P00877
Secondary accession number(s): B7U1I9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 7, 2018
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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