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P27064

- RBL_CUCSA

UniProt

P27064 - RBL_CUCSA

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

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.

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

Cofactori

Mg2+By similarityNote: Binds 1 Mg(2+) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Substrate; in homodimeric partnerBy similarity
Binding sitei173 – 1731SubstrateBy similarity
Active sitei175 – 1751Proton acceptorBy similarity
Binding sitei177 – 1771SubstrateBy similarity
Metal bindingi201 – 2011Magnesium; via carbamate groupBy similarity
Metal bindingi203 – 2031MagnesiumBy similarity
Metal bindingi204 – 2041MagnesiumBy similarity
Active sitei294 – 2941Proton acceptorBy similarity
Binding sitei295 – 2951SubstrateBy similarity
Binding sitei327 – 3271SubstrateBy similarity
Sitei334 – 3341Transition state stabilizerBy similarity
Binding sitei379 – 3791SubstrateBy 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-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 221 PublicationPRO_0000031195
Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_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-carboxylysineBy similarity
Disulfide bondi247 – 247Interchain; in linked formBy 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

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliP27064.
SMRiP27064. Positions 18-473.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP
60 70 80 90 100
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYGIEPV AGEENQYIAY
110 120 130 140 150
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PTAYIKTFQG
160 170 180 190 200
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL NATAGTCEEM
260 270 280 290 300
MKRAIFAREL GAPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR
360 370 380 390 400
DDFVEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL
410 420 430 440 450
QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK
460 470
WSPELAAACE VWKEIKFEFE AMDTL
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171F → V in AAA84187. 1 PublicationCurated
Sequence conflicti117 – 1171F → V in AAL35646. 1 PublicationCurated
Sequence conflicti237 – 2393GHY → DI in CAJ00766. (PubMed:17607527)Curated
Sequence conflicti456 – 4627AAACEVW → VCVTWRKYG in CAJ00766. (PubMed:17607527)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 91 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).By similarity

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3