SubmitCancel

Skip Header

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

G1D766

- G1D766_RICCO

UniProt

G1D766 - G1D766_RICCO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ribulose bisphosphate carboxylase large chain
Gene
rbcL, RCOM_ORF00051
Organism
Ricinus communis (Castor bean)
Status
Unreviewed - Annotation score: 4 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. Both reactions occur simultaneously and in competition at the same active site By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei173 – 1731Substrate By similarityUniRule annotation
Active sitei175 – 1751Proton acceptor By similarityUniRule annotation
Binding sitei177 – 1771Substrate By similarityUniRule annotation
Metal bindingi201 – 2011Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi203 – 2031Magnesium By similarityUniRule annotation
Metal bindingi204 – 2041Magnesium By similarityUniRule annotation
Active sitei294 – 2941Proton acceptor By similarityUniRule annotation
Binding sitei295 – 2951Substrate By similarityUniRule annotation
Binding sitei327 – 3271Substrate By similarityUniRule annotation
Sitei334 – 3341Transition state stabilizer By similarityUniRule annotation
Binding sitei379 – 3791Substrate By similarityUniRule 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)
Taxonomic identifieri3988 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus
ProteomesiUP000008311: Chloroplast

Subcellular locationi

Plastidchloroplast By similarity 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 – 22 By similarityUniRule annotation

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylproline By similarityUniRule annotation
Modified residuei14 – 141N6,N6,N6-trimethyllysine By similarityUniRule annotation
Modified residuei201 – 2011N6-carboxylysine By similarityUniRule annotation
Disulfide bondi247 – 247Interchain; in linked form By similarityUniRule 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 By similarity.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 By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliG1D766.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP    50
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEENQFIAY 100
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYTKTFQG 150
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
KDDENVNSQP FMRWRDRFLF CAEAIYKAQA ETGEIKGHYL NATAGTCEEM 250
IKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV 300
IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERD ITLGFVDLLR 350
DDFIEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL 400
QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREAGK 450
WSPELAAACE VWKEIKFEFP AMDTL 475
Length:475
Mass (Da):52,638
Last modified:October 19, 2011 - v1
Checksum:iE3685F131A17C4E6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
JF937588 Genomic DNA. Translation: AEJ82563.1 .
RefSeqi YP_005090186.1. NC_016736.1.

3D structure databases

ProteinModelPortali G1D766.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 11542325.
KEGGi rcu:RCOM_ORF00051.

Phylogenomic databases

KOi K01601.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

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: July 9, 2014
This is version 15 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" By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi