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P00877

- RBL_CHLRE

UniProt

P00877 - RBL_CHLRE

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
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+Note: Binds 1 Mg(2+) ion per subunit.

Sites

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

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

Enzyme and pathway databases

BioCyciCHLAMY:CHRECP049-MONOMER.

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
Encoded oniPlastid; Chloroplast
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
ProteomesiUP000006906: Chloroplast

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_0000031175
Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_0000031176Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylproline1 Publication
Modified residuei104 – 10414-hydroxyproline1 Publication
Modified residuei151 – 15114-hydroxyproline
Modified residuei201 – 2011N6-carboxylysine2 Publications
Disulfide bondi247 – 247Interchain; in linked form
Modified residuei256 – 2561S-methylcysteine1 Publication
Modified residuei369 – 3691S-methylcysteine1 Publication

Post-translational modificationi

The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bond reported in 1IR2 may be the result of oxidation during crystallization.By similarity
The electron density found in the position of Thr-471 (PubMed:11866526 only) suggests it is either O-methylthreonine, or Ile, which may be produced by RNA editing.

Keywords - PTMi

Acetylation, Disulfide bond, Hydroxylation, Methylation

Proteomic databases

PRIDEiP00877.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.2 Publications

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 244Combined sources
Beta strandi36 – 449Combined sources
Helixi50 – 6011Combined sources
Turni61 – 633Combined sources
Beta strandi66 – 683Combined sources
Helixi70 – 745Combined sources
Helixi77 – 804Combined sources
Beta strandi83 – 897Combined sources
Beta strandi93 – 953Combined sources
Beta strandi97 – 1037Combined sources
Helixi105 – 1073Combined sources
Helixi113 – 1219Combined sources
Helixi124 – 1263Combined sources
Beta strandi130 – 13910Combined sources
Helixi142 – 1454Combined sources
Helixi155 – 1628Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi175 – 1784Combined sources
Helixi182 – 19413Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi207 – 2093Combined sources
Helixi214 – 23219Combined sources
Beta strandi237 – 2415Combined sources
Helixi247 – 26014Combined sources
Beta strandi263 – 2686Combined sources
Helixi269 – 2724Combined sources
Helixi274 – 28714Combined sources
Beta strandi290 – 2945Combined sources
Helixi298 – 3025Combined sources
Beta strandi305 – 3095Combined sources
Helixi311 – 32111Combined sources
Beta strandi324 – 3274Combined sources
Beta strandi331 – 3355Combined sources
Helixi339 – 35012Combined sources
Beta strandi352 – 3543Combined sources
Helixi358 – 3603Combined sources
Beta strandi375 – 3817Combined sources
Helixi384 – 3863Combined sources
Helixi387 – 3948Combined sources
Beta strandi396 – 4016Combined sources
Helixi404 – 4074Combined sources
Helixi413 – 43220Combined sources
Helixi437 – 45115Combined sources
Helixi453 – 46210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GK8X-ray1.40A/C/E/G1-475[»]
1IR2X-ray1.84A/B/C/D/E/F/G/H/S/T/U/V/W/X/Y/Z1-475[»]
1UW9X-ray2.05A/B/E/H/K/O/R/V1-475[»]
1UWAX-ray2.30A/B/E/H/K/O/R/V1-475[»]
1UZDX-ray2.40A/B/E/H/K/O/R/V1-475[»]
1UZHX-ray2.20A/B/E/H/K/O/R/V1-475[»]
2V63X-ray1.80A/B/C/D/E/F/G/H1-475[»]
2V67X-ray2.00A/B/C/D/E/F/G/H1-475[»]
2V68X-ray2.30A/B/C/D/E/F/G/H1-475[»]
2V69X-ray2.80A/B/C/D/E/F/G/H1-475[»]
2V6AX-ray1.50A/B/C/D/E/F/G/H1-475[»]
2VDHX-ray2.30A/B/C/D/E/F/G/H1-475[»]
2VDIX-ray2.65A/B/C/D/E/F/G/H1-475[»]
ProteinModelPortaliP00877.
SMRiP00877. Positions 7-475.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00877.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP00877.
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.

P00877-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVPQTETKAG AGFKAGVKDY RLTYYTPDYV VRDTDILAAF RMTPQLGVPP
60 70 80 90 100
EECGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV PGEDNQYIAY
110 120 130 140 150
VAYPIDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYVKTFVG
160 170 180 190 200
PPHGIQVERD KLNKYGRGLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFLF VAEAIYKAQA ETGEVKGHYL NATAGTCEEM
260 270 280 290 300
MKRAVCAKEL GVPIIMHDYL TGGFTANTSL AIYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQRNHGIH FRVLAKALRM SGGDHLHSGT VVGKLEGERE VTLGFVDLMR
360 370 380 390 400
DDYVEKDRSR GIYFTQDWCS MPGVMPVASG GIHVWHMPAL VEIFGDDACL
410 420 430 440 450
QFGGGTLGHP WGNAPGAAAN RVALEACTQA RNEGRDLARE GGDVIRSACK
460 470
WSPELAAACE VWKEIKFEFD TIDKL
Length:475
Mass (Da):52,543
Last modified:July 21, 1986 - v1
Checksum:i5A9BFD394CF7D4D4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461L → P in strain: 137c and CC-503.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01399 Genomic DNA. Translation: AAA84449.1.
FJ423446 Genomic DNA. Translation: ACJ50136.1.
BK000554 Genomic DNA. Translation: DAA00950.1.
PIRiA01097. RKKML.
RefSeqiNP_958405.1. NC_005353.1.

Genome annotation databases

EnsemblPlantsiDAA00950; DAA00950; DAA00950.
GeneIDi2717040.
KEGGicre:ChreCp049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01399 Genomic DNA. Translation: AAA84449.1 .
FJ423446 Genomic DNA. Translation: ACJ50136.1 .
BK000554 Genomic DNA. Translation: DAA00950.1 .
PIRi A01097. RKKML.
RefSeqi NP_958405.1. NC_005353.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GK8 X-ray 1.40 A/C/E/G 1-475 [» ]
1IR2 X-ray 1.84 A/B/C/D/E/F/G/H/S/T/U/V/W/X/Y/Z 1-475 [» ]
1UW9 X-ray 2.05 A/B/E/H/K/O/R/V 1-475 [» ]
1UWA X-ray 2.30 A/B/E/H/K/O/R/V 1-475 [» ]
1UZD X-ray 2.40 A/B/E/H/K/O/R/V 1-475 [» ]
1UZH X-ray 2.20 A/B/E/H/K/O/R/V 1-475 [» ]
2V63 X-ray 1.80 A/B/C/D/E/F/G/H 1-475 [» ]
2V67 X-ray 2.00 A/B/C/D/E/F/G/H 1-475 [» ]
2V68 X-ray 2.30 A/B/C/D/E/F/G/H 1-475 [» ]
2V69 X-ray 2.80 A/B/C/D/E/F/G/H 1-475 [» ]
2V6A X-ray 1.50 A/B/C/D/E/F/G/H 1-475 [» ]
2VDH X-ray 2.30 A/B/C/D/E/F/G/H 1-475 [» ]
2VDI X-ray 2.65 A/B/C/D/E/F/G/H 1-475 [» ]
ProteinModelPortali P00877.
SMRi P00877. Positions 7-475.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P00877.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi DAA00950 ; DAA00950 ; DAA00950 .
GeneIDi 2717040.
KEGGi cre:ChreCp049.

Phylogenomic databases

InParanoidi P00877.
KOi K01601.

Enzyme and pathway databases

BioCyci CHLAMY:CHRECP049-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00877.

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. "Sequence of the chloroplast DNA region of Chlamydomonas reinhardii containing the gene of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes."
    Dron M., Rahire M., Rochaix J.-D.
    J. Mol. Biol. 162:775-793(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CARBAMYLATION AT LYS-201.
  2. "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome: addressing the mutational-hazard hypothesis."
    Smith D.R., Lee R.W.
    BMC Evol. Biol. 9:120-120(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CC-503.
  3. "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 3-14, ACETYLATION AT PRO-3.
  4. "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats."
    Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., Stern D.B.
    Plant Cell 14:2659-2679(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, COMPLETE PLASTID GENOME.
  5. "First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii."
    Taylor T.C., Backlund A., Bjorhall K., Spreitzer R.J., Andersson I.
    J. Biol. Chem. 276:48159-48164(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP, HYDROXYLATION AT PRO-104 AND 151, CARBAMYLATION AT LYS-201, METHYLATION AT CYS-256 AND CYS-369.
    Strain: 2137.
  6. "Crystal structure of activated ribulose-1,5-bisphosphate carboxylase/oxygenase from green alga Chlamydomonas reinhardtii complexed with 2-carboxyarabinitol-1,5-bisphosphate."
    Mizohata E., Matsumura H., Okano Y., Kumei M., Takuma H., Onodera J., Kato K., Shibata N., Inoue T., Yokota A., Kai Y.
    J. Mol. Biol. 316:679-691(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH THE TRANSITION-STATE ANALOG 2-CABP.
    Strain: 137c / CC-125.

Entry informationi

Entry nameiRBL_CHLRE
AccessioniPrimary (citable) accession number: P00877
Secondary accession number(s): B7U1I9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 121 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".

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3