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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Ricinus communis (Castor bean)
Status
Unreviewed-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Substrate; in homodimeric partnerUniRule annotation
Binding sitei173 – 1731SubstrateUniRule annotation
Active sitei175 – 1751Proton acceptorUniRule annotation
Binding sitei177 – 1771SubstrateUniRule annotation
Metal bindingi201 – 2011Magnesium; via carbamate groupUniRule annotation
Metal bindingi203 – 2031MagnesiumUniRule annotation
Metal bindingi204 – 2041MagnesiumUniRule annotation
Active sitei294 – 2941Proton acceptorUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei327 – 3271SubstrateUniRule annotation
Sitei334 – 3341Transition state stabilizerUniRule annotation
Binding sitei379 – 3791SubstrateUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

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
ORF Names:RCOM_ORF00051Imported
Encoded oniPlastid; ChloroplastImported
OrganismiRicinus communis (Castor bean)Imported
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus
ProteomesiUP000008311: Chloroplast

Subcellular locationi

Plastidchloroplast UniRule annotation

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

ChloroplastUniRule annotationImported, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22UniRule annotation

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylprolineUniRule annotation
Modified residuei14 – 141N6,N6,N6-trimethyllysineUniRule annotation
Modified residuei201 – 2011N6-carboxylysineUniRule annotation
Disulfide bondi247 – 247Interchain; 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

AcetylationUniRule annotation, Disulfide bondUniRule annotation, MethylationUniRule annotation

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

ProteinModelPortaliG1D766.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiG1D766.
KOiK01601.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[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.

G1D766-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP
60 70 80 90 100
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEENQFIAY
110 120 130 140 150
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYTKTFQG
160 170 180 190 200
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFLF CAEAIYKAQA ETGEIKGHYL NATAGTCEEM
260 270 280 290 300
IKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERD ITLGFVDLLR
360 370 380 390 400
DDFIEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL
410 420 430 440 450
QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREAGK
460 470
WSPELAAACE VWKEIKFEFP AMDTL
Length:475
Mass (Da):52,638
Last modified:October 19, 2011 - v1
Checksum:iE3685F131A17C4E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JF937588 Genomic DNA. Translation: AEJ82563.1.
RefSeqiYP_005090186.1. NC_016736.1.

Genome annotation databases

GeneIDi11542325.
KEGGircu:RCOM_ORF00051.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JF937588 Genomic DNA. Translation: AEJ82563.1.
RefSeqiYP_005090186.1. NC_016736.1.

3D structure databases

ProteinModelPortaliG1D766.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi11542325.
KEGGircu:RCOM_ORF00051.

Phylogenomic databases

InParanoidiG1D766.
KOiK01601.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. HaleImported.

Entry informationi

Entry nameiG1D766_RICCO
AccessioniPrimary (citable) accession number: G1D766
Entry historyi
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: January 7, 2015
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.