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P04717

- RBL_PEA

UniProt

P04717 - RBL_PEA

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Pisum sativum (Garden pea)
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
Encoded oniPlastid; Chloroplast
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

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_0000031333
Chaini3 – 475473Ribulose bisphosphate carboxylase large chainPRO_0000031334Add
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

Proteomic databases

PRIDEiP04717.

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

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 strandi91 – 944Combined sources
Beta strandi97 – 1037Combined sources
Helixi105 – 1073Combined sources
Helixi113 – 1219Combined sources
Helixi124 – 1263Combined sources
Beta strandi130 – 13910Combined sources
Helixi142 – 1454Combined sources
Beta strandi151 – 1533Combined 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 strandi399 – 4013Combined sources
Helixi404 – 4074Combined sources
Helixi413 – 43220Combined sources
Helixi437 – 44812Combined sources
Turni449 – 4513Combined sources
Helixi453 – 46210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HHHX-ray2.20A/B/C/D1-475[»]
4MKVX-ray2.15A/B/C/D12-469[»]
ProteinModelPortaliP04717.
SMRiP04717. Positions 9-475.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

P04717-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPQTETKAK VGFKAGVKDY KLTYYTPDYQ TKDTDILAAF RVTPQPGVPP
60 70 80 90 100
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYEIEPV PGEDNQFIAY
110 120 130 140 150
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PYAYVKTFQG
160 170 180 190 200
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL NATAGTCEEM
260 270 280 290 300
LKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGERE ITLGFVDLLR
360 370 380 390 400
DDYIKKDRSR GIYFTQDWVS LPGVIPVASG GIHVWHMPAL TEIFGDDSVL
410 420 430 440 450
QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNAIIREACK
460 470
WSPELAAACE VWKEIKFEFP AMDTL
Length:475
Mass (Da):52,763
Last modified:December 1, 1992 - v3
Checksum:i1F673855DD921DF9
GO

Sequence cautioni

The sequence CAA27483.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03853 Genomic DNA. Translation: CAA27483.1. Different initiation.
PIRiA24471. RKPMLC.
RefSeqiYP_003587524.1. NC_014057.1.

Genome annotation databases

GeneIDi9073048.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03853 Genomic DNA. Translation: CAA27483.1 . Different initiation.
PIRi A24471. RKPMLC.
RefSeqi YP_003587524.1. NC_014057.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4HHH X-ray 2.20 A/B/C/D 1-475 [» ]
4MKV X-ray 2.15 A/B/C/D 12-469 [» ]
ProteinModelPortali P04717.
SMRi P04717. Positions 9-475.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P04717.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 9073048.

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. "Sequence of the gene for the large subunit of ribulose 1,5-bisphosphate carboxylase from pea chloroplasts."
    Zurawski G., Whitfeld P.R., Bottomley W.
    Nucleic Acids Res. 14:3975-3976(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.

Entry informationi

Entry nameiRBL_PEA
AccessioniPrimary (citable) accession number: P04717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 1, 1992
Last modified: November 26, 2014
This is version 100 of the entry and version 3 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

3D-structure, Direct protein sequencing

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