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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, 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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-27641N.
MINTiMINT-1522611.

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 24Combined sources4
Beta strandi36 – 44Combined sources9
Helixi50 – 59Combined sources10
Turni60 – 63Combined sources4
Beta strandi66 – 68Combined sources3
Helixi70 – 74Combined sources5
Helixi77 – 80Combined sources4
Beta strandi83 – 89Combined sources7
Beta strandi93 – 95Combined sources3
Beta strandi97 – 103Combined sources7
Helixi105 – 107Combined sources3
Helixi113 – 121Combined sources9
Helixi124 – 126Combined sources3
Beta strandi130 – 139Combined sources10
Helixi142 – 145Combined sources4
Helixi155 – 162Combined sources8
Beta strandi169 – 171Combined sources3
Beta strandi175 – 178Combined sources4
Helixi182 – 194Combined sources13
Beta strandi198 – 201Combined sources4
Beta strandi207 – 209Combined sources3
Helixi214 – 232Combined sources19
Beta strandi237 – 241Combined sources5
Helixi247 – 260Combined sources14
Beta strandi263 – 268Combined sources6
Helixi269 – 272Combined sources4
Helixi274 – 287Combined sources14
Beta strandi290 – 294Combined sources5
Helixi298 – 302Combined sources5
Beta strandi305 – 309Combined sources5
Helixi311 – 321Combined sources11
Beta strandi324 – 327Combined sources4
Beta strandi331 – 335Combined sources5
Helixi339 – 350Combined sources12
Beta strandi352 – 354Combined sources3
Helixi358 – 360Combined sources3
Beta strandi375 – 381Combined sources7
Helixi384 – 386Combined sources3
Helixi387 – 394Combined sources8
Beta strandi396 – 401Combined sources6
Helixi404 – 407Combined sources4
Helixi413 – 432Combined sources20
Helixi437 – 448Combined sources12
Turni449 – 451Combined sources3
Helixi453 – 462Combined sources10

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...

Miscellaneous databases

EvolutionaryTraceiP00875.

Family & Domainsi

Sequence similaritiesi

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.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

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.

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.
MINTiMINT-1522611.

Protein family/group databases

Allergomei3814. Spi o RuBisCO.

Proteomic databases

PRIDEiP00875.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2715621.

Enzyme and pathway databases

BRENDAi4.1.1.39. 5812.

Miscellaneous databases

EvolutionaryTraceiP00875.
PROiP00875.

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.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRBL_SPIOL
AccessioniPrimary (citable) accession number: P00875
Secondary accession number(s): Q9M3L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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".

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.