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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Arabidopsis thaliana (Mouse-ear cress)
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.UniRule annotation

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".UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei65SubstrateCombined sources1 Publication1
Binding sitei123Substrate; in homodimeric partnerUniRule annotationCombined sources1 Publication1
Active sitei175Proton acceptorUniRule annotation1
Metal bindingi201Magnesium; via carbamate groupUniRule annotationCombined sources1 Publication1
Metal bindingi203MagnesiumUniRule annotationCombined sources1 Publication1
Metal bindingi204MagnesiumUniRule annotationCombined sources1 Publication1
Active sitei294Proton acceptorUniRule annotation1
Binding sitei327SubstrateUniRule annotationCombined sources1 Publication1
Binding sitei334SubstrateCombined sources1 Publication1
Sitei334Transition state stabilizerUniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • photorespiration Source: UniProtKB-KW
  • reductive pentose-phosphate cycle Source: UniProtKB-KW
  • response to abscisic acid Source: TAIR
  • response to cadmium ion Source: TAIR

Keywordsi

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

Enzyme and pathway databases

BioCyciARA:ATCG00490-MONOMER
MetaCyc:ATCG00490-MONOMER
BRENDAi4.1.1.39 399

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:rbcLUniRule annotation
Ordered Locus Names:AtCg00490
Encoded oniPlastid; Chloroplast
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chloroplast

Organism-specific databases

AraportiATCG00490
TAIRilocus:504954672 ATCG00490

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_00000311191 – 2UniRule annotationCombined sources2
ChainiPRO_00000311203 – 479Ribulose bisphosphate carboxylase large chainAdd BLAST477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylprolineCombined sources1
Modified residuei201N6-carboxylysineUniRule annotationCombined sources1 Publication1
Modified residuei208PhosphoserineCombined sources1
Disulfide bondi247Interchain; in linked formUniRule annotation
Modified residuei330PhosphothreonineCombined sources1

Post-translational modificationi

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.UniRule annotation

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiO03042
PRIDEiO03042

2D gel databases

SWISS-2DPAGEiO03042

PTM databases

iPTMnetiO03042

Expressioni

Gene expression databases

ExpressionAtlasiO03042 baseline and differential
GenevisibleiO03042 AT

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers (PubMed:29372894). Interacts with RBCX1 and RBCX1 (PubMed:21922322).2 Publications

Protein-protein interaction databases

BioGridi29958, 5 interactors
IntActiO03042, 2 interactors
MINTiO03042
STRINGi3702.ATCG00490.1

Structurei

Secondary structure

1479
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 24Combined sources4
Beta strandi36 – 44Combined sources9
Helixi50 – 60Combined sources11
Turni61 – 63Combined sources3
Helixi70 – 74Combined sources5
Helixi77 – 80Combined sources4
Beta strandi83 – 89Combined sources7
Beta strandi97 – 103Combined sources7
Helixi105 – 107Combined sources3
Helixi113 – 121Combined sources9
Helixi124 – 126Combined sources3
Beta strandi130 – 139Combined sources10
Helixi142 – 145Combined sources4
Beta strandi151 – 153Combined sources3
Helixi155 – 162Combined sources8
Beta strandi169 – 171Combined sources3
Beta strandi175 – 178Combined sources4
Helixi182 – 193Combined sources12
Turni194 – 196Combined sources3
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 strandi307 – 309Combined sources3
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
5IU0X-ray1.50A/B1-479[»]
ProteinModelPortaliO03042
SMRiO03042
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni173 – 177Substrate bindingCombined sources1 Publication5
Regioni201 – 204Substrate bindingCombined sources1 Publication4
Regioni294 – 295Substrate bindingCombined sources1 Publication2
Regioni379 – 381Substrate bindingCombined sources1 Publication3

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG410IIVP Eukaryota
COG1850 LUCA
HOGENOMiHOG000230831
InParanoidiO03042
KOiK01601
OMAiEYRETYW
OrthoDBiEOG093607MT

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
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.

O03042-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPQTETKAS VGFKAGVKEY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP
60 70 80 90 100
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEETQFIAY
110 120 130 140 150
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL AALRLEDLRI PPAYTKTFQG
160 170 180 190 200
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL NATAGTCEEM
260 270 280 290 300
IKRAVFAREL GVPIVMHDYL TGGFTANTSL SHYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGDRE STLGFVDLLR
360 370 380 390 400
DDYVEKDRSR GIFFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL
410 420 430 440 450
QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLAVE GNEIIREACK
460 470
WSPELAAACE VWKEITFNFP TIDKLDGQE
Length:479
Mass (Da):52,955
Last modified:July 1, 1997 - v1
Checksum:i3086705F3C8FEF75
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91966 Genomic DNA Translation: AAB68400.1
AP000423 Genomic DNA Translation: BAA84393.1
AB003522 Genomic DNA Translation: BAA20946.1
D88901 Genomic DNA Translation: BAA19595.1
RefSeqiNP_051067.1, NC_000932.1

Genome annotation databases

EnsemblPlantsiATCG00490.1; ATCG00490.1; ATCG00490
GeneIDi844754
GrameneiATCG00490.1; ATCG00490.1; ATCG00490
KEGGiath:ArthCp030

Similar proteinsi

Entry informationi

Entry nameiRBL_ARATH
AccessioniPrimary (citable) accession number: O03042
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: April 25, 2018
This is version 156 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, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health