Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Lupinus albus (White lupine) (Lupinus termis)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 sitei114Substrate; in homodimeric partnerUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Active sitei166Proton acceptorUniRule annotation1
Binding sitei168SubstrateUniRule annotation1
Metal bindingi192Magnesium; via carbamate groupUniRule annotation1
Metal bindingi194MagnesiumUniRule annotation1
Metal bindingi195MagnesiumUniRule annotation1
Active sitei285Proton acceptorUniRule annotation1
Binding sitei286SubstrateUniRule annotation1
Binding sitei318SubstrateUniRule annotation1
Sitei325Transition state stabilizerUniRule annotation1
Binding sitei370SubstrateUniRule annotation1

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 chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:rbcLUniRule annotation
Encoded oniPlastid; Chloroplast
OrganismiLupinus albus (White lupine) (Lupinus termis)
Taxonomic identifieri3870 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeGenisteaeLupinus

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
ChainiPRO_0000062508‹1 – ›455Ribulose bisphosphate carboxylase large chainAdd BLAST›455

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5N6,N6,N6-trimethyllysineUniRule annotation1
Modified residuei192N6-carboxylysineUniRule annotation1
Disulfide bondi238Interchain; in linked formUniRule annotation

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

Disulfide bond, Methylation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP92397
SMRiP92397
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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: Fragment.

P92397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SVGFKAGVKD YKLTYYTPDY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA
60 70 80 90 100
ESSTGTWTTV WTDGLTSLDR YKGRCYHIEP VAGEENQFIA YVAYPLDLFE
110 120 130 140 150
EGSVTNMFTS IVGNVFGFKA LRALRLEDLR IPNAYVKTFQ GPPHGIQVER
160 170 180 190 200
DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF TKDDENVNSQ
210 220 230 240 250
PFMRWRDRFL FCAEALYKAQ AETGEIKGHY LNATAGTCEE MIKRAVFARE
260 270 280 290 300
LGVPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM
310 320 330 340 350
HFRVLAKALR LSGGDHIHSG TVVGKLEGER EITLGFVDLL RDDFVEKDRS
360 370 380 390 400
RGIYFTQDWV SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH
410 420 430 440 450
PWGNAPGAVA NRVALEACVQ ARNEGRDLAS EGNQIIREAS KWSPELAAAC

EVWKE
Length:455
Mass (Da):50,315
Last modified:May 1, 1997 - v1
Checksum:iFC9AD8CF670CE339
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei4551

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70068 Genomic DNA Translation: CAA93927.1

Similar proteinsi

Entry informationi

Entry nameiRBL_LUPAL
AccessioniPrimary (citable) accession number: P92397
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: May 23, 2018
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health