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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Hydrophyllum virginianum (Eastern waterleaf)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

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

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, 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
OrganismiHydrophyllum virginianum (Eastern waterleaf)
Taxonomic identifieri4134 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsBoraginalesHydrophyllaceaeHydrophyllum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000062494‹1 – 467Ribulose bisphosphate carboxylase large chainAdd BLAST›467

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

Proteomic databases

PRIDEiP28425.

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

ProteinModelPortaliP28425.
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.
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: Fragment.

P28425-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SVGFKAGVKE YKLTYYTPEY ETKDTDILAA FRVSPQPGVP PEEAGAAVAA
60 70 80 90 100
ESSTGTWTTV WTDGLTNLDR YKGRCYHIDP VLGEEDQYIA YVAYPLDLFE
110 120 130 140 150
EGSVTNMFTS IVGNVFGFKA LRALRLEDLR IPTAYVKTFQ GPPHGIQVER
160 170 180 190 200
DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF TKDDENVNSQ
210 220 230 240 250
PFMRWRDRLL FCAEAIFKSQ AETGEIKGHY LNATAGNCEE MMKRAVFARE
260 270 280 290 300
LGVPIVMHDY LTGGFTANTT LASYCRDNGL LLHIHRAMHA VIDRQKNHGI
310 320 330 340 350
HFRVLAKALR MSGGDHIHSG TVVGKLEGER NITLSFVVLL RDDYIEKDRS
360 370 380 390 400
RGIFFTQDWV SLPGVLPVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH
410 420 430 440 450
PWGNAPGAVA NRVSLEACVQ ARNEGRDLAR EGNDIIREAC KWSPELAAAC
460
EVWKEIKFEF TDMDTLD
Length:467
Mass (Da):51,905
Last modified:December 1, 1992 - v1
Checksum:iAFD680117497BD9B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01927 Genomic DNA. Translation: AAA84324.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01927 Genomic DNA. Translation: AAA84324.2.

3D structure databases

ProteinModelPortaliP28425.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP28425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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_HYDVI
AccessioniPrimary (citable) accession number: P28425
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 30, 2016
This is version 84 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".UniRule annotation

Documents

  1. 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.