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P00876 (RBL_TOBAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain
Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:rbcL
Synonyms:rbcA
Encoded onPlastid; Chloroplast
OrganismNicotiana tabacum (Common tobacco)
Taxonomic identifier4097 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit.

Subunit structure

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

Subcellular location

Plastid › chloroplast HAMAP-Rule MF_01338.

Post-translational modification

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 bonds reported in 3RUB and 4RUB may be the result of oxidation during crystallization. HAMAP-Rule MF_01338

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". HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22 HAMAP-Rule MF_01338
PRO_0000031427
Chain3 – 477475Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000031428

Sites

Active site1751Proton acceptor
Active site2941Proton acceptor
Metal binding2011Magnesium; via carbamate group
Metal binding2031Magnesium
Metal binding2041Magnesium
Binding site1231Substrate; in homodimeric partner
Binding site1731Substrate
Binding site1771Substrate
Binding site2951Substrate
Binding site3271Substrate
Binding site3791Substrate
Site3341Transition state stabilizer

Amino acid modifications

Modified residue31N-acetylproline HAMAP-Rule MF_01338
Modified residue141N6,N6,N6-trimethyllysine Ref.4
Modified residue2011N6-carboxylysine HAMAP-Rule MF_01338
Disulfide bond247Interchain; in linked form HAMAP-Rule MF_01338

Natural variations

Natural variant3941F → V. Ref.3
Natural variant4051G → M. Ref.3

Experimental info

Sequence conflict2841C → G AA sequence Ref.3
Sequence conflict3771V → E in AAD15025. Ref.1

Secondary structure

1 ...................................................................................... 477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00876 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 232D54E42263198F

FASTA47752,898
        10         20         30         40         50         60 
MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PPAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL 

       250        260        270        280        290        300 
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFVEQDRSR 

       370        380        390        400        410        420 
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 

       430        440        450        460        470 
RVALEACVKA RNEGRDLAQE GNEIIREACK WSPELAAACE VWKEIVFNFA AVDVLDK

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of the tobacco chloroplast gene for the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase."
Shinozaki K., Sugiura M.
Gene 20:91-102(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression."
Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N., Matsubayashi T., Zaita N., Chunwongse J., Obokata J., Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M., Deno H., Kamogashira T., Yamada K., Kusuda J. expand/collapse author list , Takaiwa F., Kato A., Tohdoh N., Shimada H., Sugiura M.
EMBO J. 5:2043-2049(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Bright Yellow 4.
[3]"Amino-acid sequence of the large subunit of D-ribulose bisphosphate carboxylase/oxygenase from Nicotiana tabacum."
Amiri I., Salnikow J., Vater J.
Biochim. Biophys. Acta 784:116-123(1984)
Cited for: PROTEIN SEQUENCE OF 5-477, VARIANTS VAL-394 AND MET-405.
[4]"Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase."
Houtz R.L., Stults J.T., Mulligan R.M., Tolbert N.E.
Proc. Natl. Acad. Sci. U.S.A. 86:1855-1859(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14.
[5]"A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum in the activated state."
Suh S.W., Cascio D., Chapman M.S., Eisenberg D.
J. Mol. Biol. 197:363-365(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[6]"Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0-A resolution."
Curmi P.M.G., Cascio D., Sweet R.M., Eisenberg D., Schreuder H.
J. Biol. Chem. 267:16980-16989(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]"The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate."
Duff A.P., Andrews T.J., Curmi P.M.G.
J. Mol. Biol. 298:903-916(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 3-477.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J01450 Genomic DNA. Translation: AAD15025.1.
Z00044 Genomic DNA. Translation: CAA77361.1.
PIRRKNTL. A01095.
RefSeqNP_054507.1. NC_001879.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ7X-ray2.45L3-477[»]
1RLCX-ray2.70L1-477[»]
1RLDX-ray2.50A/B22-467[»]
3RUBX-ray2.00L1-477[»]
4RUBX-ray2.70A/B/C/D1-477[»]
ProteinModelPortalP00876.
SMRP00876. Positions 9-472.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-42221N.
MINTMINT-1176576.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID800513.

Phylogenomic databases

ProtClustDBCHL00040.

Enzyme and pathway databases

SABIO-RKP00876.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00876.

Entry information

Entry nameRBL_TOBAC
AccessionPrimary (citable) accession number: P00876
Secondary accession number(s): Q32716
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents