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.

P27064

- RBL_CUCSA

UniProt

P27064 - RBL_CUCSA

(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, CsCp048
Organism
Cucumis sativus (Cucumber)
Status
Reviewed - Annotation score: 5 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.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 similarity
Binding sitei173 – 1731Substrate By similarity
Active sitei175 – 1751Proton acceptor By similarity
Binding sitei177 – 1771Substrate By similarity
Metal bindingi201 – 2011Magnesium; via carbamate group By similarity
Metal bindingi203 – 2031Magnesium By similarity
Metal bindingi204 – 2041Magnesium By similarity
Active sitei294 – 2941Proton acceptor By similarity
Binding sitei295 – 2951Substrate By similarity
Binding sitei327 – 3271Substrate By similarity
Sitei334 – 3341Transition state stabilizer By similarity
Binding sitei379 – 3791Substrate By similarity

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

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 chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:rbcL
Ordered Locus Names:CsCp048
Encoded oniPlastid; Chloroplast
OrganismiCucumis sativus (Cucumber)
Taxonomic identifieri3659 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22UniRule annotationPRO_0000031195
Chaini3 – 475473Ribulose bisphosphate carboxylase large chainUniRule annotationPRO_0000031196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylproline1 Publication
Modified residuei14 – 141N6,N6,N6-trimethyllysine1 Publication
Modified residuei201 – 2011N6-carboxylysine By similarity
Disulfide bondi247 – 247Interchain; in linked form By similarity

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

Acetylation, 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 By similarity.

Structurei

3D structure databases

ProteinModelPortaliP27064.
SMRiP27064. Positions 18-473.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27064-1 [UniParc]FASTAAdd to Basket

« Hide

MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP    50
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYGIEPV AGEENQYIAY 100
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PTAYIKTFQG 150
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL NATAGTCEEM 250
MKRAIFAREL GAPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 300
IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR 350
DDFVEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL 400
QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK 450
WSPELAAACE VWKEIKFEFE AMDTL 475
Length:475
Mass (Da):52,642
Last modified:September 11, 2007 - v5
Checksum:iF03D68FF32EEB6B4
GO

Sequence cautioni

The sequence AAZ94659.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171F → V in AAA84187. 1 Publication
Sequence conflicti117 – 1171F → V in AAL35646. 1 Publication
Sequence conflicti237 – 2393GHY → DI in CAJ00766. 1 Publication
Sequence conflicti456 – 4627AAACEVW → VCVTWRKYG in CAJ00766. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ119058 Genomic DNA. Translation: AAZ94659.1. Different initiation.
AJ970307 Genomic DNA. Translation: CAJ00766.1.
DQ865975 Genomic DNA. Translation: ABI97425.1.
DQ865976 Genomic DNA. Translation: ABI98753.1.
L21937 Genomic DNA. Translation: AAA84187.1.
AF206755 Genomic DNA. Translation: AAL35646.1.
RefSeqiYP_247607.1. NC_007144.1.

Genome annotation databases

GeneIDi3429289.
KEGGicsv:3429289.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ119058 Genomic DNA. Translation: AAZ94659.1 . Different initiation.
AJ970307 Genomic DNA. Translation: CAJ00766.1 .
DQ865975 Genomic DNA. Translation: ABI97425.1 .
DQ865976 Genomic DNA. Translation: ABI98753.1 .
L21937 Genomic DNA. Translation: AAA84187.1 .
AF206755 Genomic DNA. Translation: AAL35646.1 .
RefSeqi YP_247607.1. NC_007144.1.

3D structure databases

ProteinModelPortali P27064.
SMRi P27064. Positions 18-473.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3429289.
KEGGi csv:3429289.

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

« Hide 'large scale' publications
  1. "Complete sequence and organization of the cucumber (Cucumis sativus L. cv. Baekmibaekdadagi) chloroplast genome."
    Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J., Choi D.-W., Liu J.R., Cho K.Y.
    Plant Cell Rep. 25:334-340(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Baekmibaekdadagi.
  2. "The complete structure of the cucumber (Cucumis sativus L.) chloroplast genome: its composition and comparative analysis."
    Plader W.W., Yukawa Y., Sugiura M., Malepszy S.
    Cell. Mol. Biol. Lett. 12:584-594(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Borszczagowski.
  3. "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies differences between chilling-tolerant and -susceptible cucumber lines."
    Chung S.-M., Gordon V.S., Staub J.E.
    Genome 50:215-225(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Chipper and cv. Gy14.
  4. "Posttranslational modifications in the amino-terminal region of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several plant species."
    Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.
    Plant Physiol. 98:1170-1174(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14, ACETYLATION AT PRO-3.
  5. "Phylogenetic affinites of Datiscaceae based on an analysis of nucleotide sequences from the plastid rbcL gene."
    Swensen S.M., Mullin B.C., Chase M.W.
    Syst. Bot. 19:157-168(1994)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-473.
  6. "Angiosperm phylogeny inferred from multiple genes as a tool for comparative biology."
    Soltis P.S., Soltis D.E., Chase M.W.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-473.

Entry informationi

Entry nameiRBL_CUCSA
AccessioniPrimary (citable) accession number: P27064
Secondary accession number(s): A5J1U2
, Q2QD81, Q32077, Q4VZI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 88 of the entry and version 5 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" By similarity.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi