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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Spinacia oleracea (Spinach)
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 (PubMed:2928307). 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".

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+3 PublicationsNote: Binds 1 Mg2+ ion per subunit (PubMed:2118958, PubMed:8648644, PubMed:9092835). Ca2+ can substitute but is not catalytically competent (PubMed:14596800, PubMed:9034362).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei123Substrate; in homodimeric partner1
Binding sitei173Substrate1
Active sitei175Proton acceptor1 Publication2 Publications1
Binding sitei177Substrate1
Metal bindingi201Magnesium; via carbamate group3 Publications2 Publications1
Metal bindingi203Magnesium3 Publications2 Publications1
Metal bindingi204Magnesium3 Publications2 Publications1
Active sitei294Proton acceptor1 Publication1
Binding sitei295Substrate1
Binding sitei327Substrate1
Sitei334Transition state stabilizer1 Publication1
Binding sitei379Substrate1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi4.1.1.39 5812

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
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia
Proteomesi
  • UP000054095 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

Pathology & Biotechi

Protein family/group databases

Allergomei3814 Spi o RuBisCO

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000314151 – 21 Publication2
ChainiPRO_00000314163 – 475Ribulose bisphosphate carboxylase large chainAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylproline1 Publication1
Modified residuei201N6-carboxylysine5 Publications1
Disulfide bondi247Interchain; in linked form

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 bonds reported in 1RBO may be the result of oxidation during crystallization.By similarityCurated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei14Not N6-methylated1 Publication1

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PRIDEiP00875

PTM databases

iPTMnetiP00875

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.7 Publications

Protein-protein interaction databases

DIPiDIP-27641N
IntActiP00875, 1 interactor
MINTiP00875

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP00875
SMRiP00875
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00875

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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, 1 hit
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.

P00875-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSPQTETKAS VEFKAGVKDY KLTYYTPEYE TLDTDILAAF RVSPQPGVPP
60 70 80 90 100
EEAGAAVAAE SSTGTWTTVW TDGLTNLDRY KGRCYHIEPV AGEENQYICY
110 120 130 140 150
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PVAYVKTFQG
160 170 180 190 200
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL NATAGTCEDM
260 270 280 290 300
MKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERD ITLGFVDLLR
360 370 380 390 400
DDYTEKDRSR GIYFTQSWVS TPGVLPVASG GIHVWHMPAL TEIFGDDSVL
410 420 430 440 450
QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNTIIREATK
460 470
WSPELAAACE VWKEIKFEFP AMDTV
Length:475
Mass (Da):52,740
Last modified:July 21, 1986 - v1
Checksum:i484FFFFD36BB1238
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12E → G in CAB88737 (PubMed:11292076).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00168 Genomic DNA Translation: CAA23473.1
AJ400848 Genomic DNA Translation: CAB88737.1
PIRiA01094 RKSPL
A28965
RefSeqiNP_054944.1, NC_002202.1

Genome annotation databases

GeneIDi2715621
KEGGisoe:2715621

Similar proteinsi

Cross-referencesi

Web resourcesi

Protein Spotlight

The Plant Kingdom's sloth - Issue 38 of September 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00168 Genomic DNA Translation: CAA23473.1
AJ400848 Genomic DNA Translation: CAB88737.1
PIRiA01094 RKSPL
A28965
RefSeqiNP_054944.1, NC_002202.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AA1X-ray2.20B/E/H/L1-475[»]
1AUSX-ray2.20L/M/N/O1-475[»]
1IR1X-ray1.80A/B/C/D1-475[»]
1RBOX-ray2.30B/E/H/L1-475[»]
1RCOX-ray2.30B/E/H/K/L/O/R/V1-475[»]
1RCXX-ray2.40B/E/H/K/L/O/R/V1-475[»]
1RXOX-ray2.20B/E/H/L1-475[»]
1UPMX-ray2.30B/E/H/K/L/O/R/V1-475[»]
1UPPX-ray2.30A/C/E/G1-475[»]
8RUCX-ray1.60A/C/E/G1-475[»]
ProteinModelPortaliP00875
SMRiP00875
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-27641N
IntActiP00875, 1 interactor
MINTiP00875

Protein family/group databases

Allergomei3814 Spi o RuBisCO

PTM databases

iPTMnetiP00875

Proteomic databases

PRIDEiP00875

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2715621
KEGGisoe:2715621

Phylogenomic databases

KOiK01601

Enzyme and pathway databases

BRENDAi4.1.1.39 5812

Miscellaneous databases

EvolutionaryTraceiP00875
PROiPR:P00875

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, 1 hit
SUPFAMiSSF51649 SSF51649, 1 hit
SSF54966 SSF54966, 1 hit
PROSITEiView protein in PROSITE
PS00157 RUBISCO_LARGE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRBL_SPIOL
AccessioniPrimary (citable) accession number: P00875
Secondary accession number(s): Q9M3L8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 10, 2018
This is version 157 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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