Ribulose bisphosphate carboxylase large chain precursor - Arabidopsis thaliana (Mouse-ear cress)

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O03042 (RBL_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribulose bisphosphate carboxylase large chain
Short name=RuBisCO large subunit
EC=4.1.1.39

Gene names

Name:	rbcL
Ordered Locus Names:	AtCg00490

Encoded on

Plastid; Chloroplast

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. 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 By similarity. HAMAP-Rule MF_01338
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.
Subcellular location	Plastid › chloroplast Ref.5.
Post-translational modification	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. 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" By similarity. HAMAP-Rule MF_01338
Sequence similarities	Belongs to the RuBisCO large chain family. Type I subfamily.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photorespiration Photosynthesis
Cellular component	Chloroplast Plastid
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Acetylation Disulfide bond Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	photorespiration Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast ribulose bisphosphate carboxylase complex Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 2

By similarity

PRO_0000031119

Chain

3 – 479

477

Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

PRO_0000031120

Sites

Active site

175

Proton acceptor By similarity

Active site

294

Proton acceptor By similarity

Metal binding

201

Magnesium; via carbamate group By similarity

Metal binding

203

Magnesium By similarity

Metal binding

204

Magnesium By similarity

Binding site

123

Substrate; in homodimeric partner By similarity

Binding site

173

Substrate By similarity

Binding site

177

Substrate By similarity

Binding site

295

Substrate By similarity

Binding site

327

Substrate By similarity

Binding site

379

Substrate By similarity

Site

334

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

N-acetylproline By similarity

Modified residue

N6,N6,N6-trimethyllysine By similarity

Modified residue

147

Phosphothreonine Ref.6

Modified residue

201

N6-carboxylysine By similarity

Modified residue

330

Phosphothreonine Ref.6

Disulfide bond

247

Interchain; in linked form By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O03042 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 3086705F3C8FEF75
Show »

FASTA

479

52,955

        10         20         30         40         50         60 
MSPQTETKAS VGFKAGVKEY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEETQFIAY VAYPLDLFEE GSVTNMFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL AALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

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

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

       310        320        330        340        350        360 
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGDRE STLGFVDLLR DDYVEKDRSR 

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

       430        440        450        460        470 
RVALEACVQA RNEGRDLAVE GNEIIREACK WSPELAAACE VWKEITFNFP TIDKLDGQE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence of ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit from Arabidopsis thaliana." Zhu G., Jensen R.G., Bohnert H.J. Plant Gene Register PGR97-074 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[2]	"Complete structure of the chloroplast genome of Arabidopsis thaliana." Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S. DNA Res. 6:283-290(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Evidence for transcriptional regulation of plastid photosynthesis genes in Arabidopsis thaliana roots." Isono K., Niwa Y., Satoh K., Kobayashi H. Plant Physiol. 114:623-630(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49. Strain: cv. Columbia.
[4]	"Morphological, physiological and molecular genetic characterization of Arabidopsis himalaica, with reference to the analogous features of A. thaliana." Tsukaya H., Ikeda H., Yokoyama J., Matsuura K., Kuroiwa H., Kuroiwa T., Iwatsuki K. J. Plant Res. 110:15-23(1997) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-446.
[5]	"Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana." Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N. Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: cv. Wassilewskija.
[6]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND THR-330, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U91966 Genomic DNA. Translation: AAB68400.1. AP000423 Genomic DNA. Translation: BAA84393.1. AB003522 Genomic DNA. Translation: BAA20946.1. D88901 Genomic DNA. Translation: BAA19595.1.
IPI	IPI00535114.
RefSeq	NP_051067.1. NC_000932.1.
3D structure databases
ProteinModelPortal	O03042.
SMR	O03042. Positions 12-469.
ModBase	Search...
Protein-protein interaction databases
IntAct	O03042. 1 interaction.
STRING	3702.ATCG00490.1-P.
2D gel databases
SWISS-2DPAGE	O03042.
Proteomic databases
PaxDb	O03042.
PRIDE	O03042.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	ATCG00490.1; ATCG00490.1; ATCG00490.
GeneID	844754.
KEGG	ath:ArthCp030.
Organism-specific databases
TAIR	AtCg00490.
Phylogenomic databases
eggNOG	COG1850.
HOGENOM	HOG000230831.
KO	K01601.
OMA	FTQDWAS.
ProtClustDB	CHL00040.
Enzyme and pathway databases
BioCyc	MetaCyc:ATCG00490-MONOMER.
Gene expression databases
ArrayExpress	O03042.
Genevestigator	O03042.
GermOnline	ATCG00490. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.20.20.110. 1 hit. 3.30.70.150. 1 hit.
HAMAP	MF_01338. RuBisCO_L_type1.
InterPro	IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
SUPFAM	SSF51649. RuBisCO_large. 1 hit. SSF54966. RuBisCO_large. 1 hit.
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBL_ARATH

Accession

Primary (citable) accession number: O03042

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents