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O78260 (RBL_ABIVE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Encoded onPlastid; Chloroplast
OrganismAbies veitchii (Veitch fir)
Taxonomic identifier78262 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Coniferopsida › Coniferales › Pinaceae › Abies

Protein attributes

Sequence length443 AA.
Sequence statusFragment.
Protein existenceInferred from homology

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 MF_01338

Catalytic activity

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

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP 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 HAMAP MF_01338.

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 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 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

Chain‹1 – ›443›443Ribulose bisphosphate carboxylase large chain HAMAP MF_01338
PRO_0000062335

Sites

Active site1681Proton acceptor By similarity
Active site2871Proton acceptor By similarity
Metal binding1941Magnesium; via carbamate group By similarity
Metal binding1961Magnesium By similarity
Metal binding1971Magnesium By similarity
Binding site1161Substrate; in homodimeric partner By similarity
Binding site1661Substrate By similarity
Binding site1701Substrate By similarity
Binding site2881Substrate By similarity
Binding site3201Substrate By similarity
Binding site3721Substrate By similarity
Site3271Transition state stabilizer By similarity

Amino acid modifications

Modified residue71N6,N6,N6-trimethyllysine By similarity
Modified residue1941N6-carboxylysine By similarity
Disulfide bond240Interchain; in linked form By similarity

Experimental info

Non-terminal residue11
Non-terminal residue4431

Sequences

Sequence LengthMass (Da)Tools
O78260 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 73F5C0E18B60DE96

FASTA44348,906
        10         20         30         40         50         60 
KASVGFKAGV KDYRLTYYTP EYQTKDTDIL AAFRVTPQPG VPPEEAGAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDGLTSL DRYKGRCYDI EPVAGEESQF IAYVAYPLDL FEEGSVTNLF TSIVGNVFGF 

       130        140        150        160        170        180 
KALRALRLED LRIPPAYSKT FQGPPHGIQV ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENVN SQPFMRWRDR FVFCAEAINK AQAETGEIKG HYLNATAGTC 

       250        260        270        280        290        300 
EEMMKRAIFA RELGVPIVMH DYLTGGFTAN TSLAHYCRDN GLLLHIHRAM HAVIDRQRNH 

       310        320        330        340        350        360 
GMHFRVLAKA LRMSGGDHVH AGTVVGKLEG ERDVTLGFVD LLRDDFIEKD RSRGIYFTQD 

       370        380        390        400        410        420 
WVSMPGVLPV ASGGIHVWHM PALTEIFGDD SVLQFGGGTL GHPWGNAPGA VANRVAVEAC 

       430        440 
VQARNEGRDL AREGNEVIRE ACK

« Hide

References

[1]"Differentiation of mitochondrial DNA polymorphisms in populations of five Japanese Abies species."
Tsumura Y., Suyama Y.
Evolution 52:1031-1042(1998) [Agricola: IND21806043]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB015649 Genomic DNA. Translation: BAA31206.1.

3D structure databases

ProteinModelPortalO78260.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01338. RuBisCO_L_type1.
[Tree]
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
Gene3DG3DSA:3.20.20.110. RuBisCO_large. 1 hit.
G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
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...

Entry information

Entry nameRBL_ABIVE
AccessionPrimary (citable) accession number: O78260
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 28, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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