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Reviewed, UniProtKB/Swiss-Prot P28376 (RBL_ACESA)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
OrganismAcer saccharum (Sugar maple)
Taxonomic identifier4024 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Sapindales › Sapindaceae › Acer

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Protein attributes

Sequence length465 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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.

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.

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.

Sequence similarities

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 465›465Ribulose bisphosphate carboxylase large chain HAMAP MF_01338
PRO_0000062337

Sites

Active site1651Proton acceptor By similarity
Active site2841Proton acceptor By similarity
Metal binding1911Magnesium; via carbamate group By similarity
Metal binding1931Magnesium By similarity
Metal binding1941Magnesium By similarity
Binding site1131Substrate; in homodimeric partner By similarity
Binding site1631Substrate By similarity
Binding site1671Substrate By similarity
Binding site2851Substrate By similarity
Binding site3171Substrate By similarity
Binding site3691Substrate By similarity
Site3241Transition state stabilizer By similarity

Amino acid modifications

Modified residue41N6,N6,N6-trimethyllysine By similarity
Modified residue1911N6-carboxylysine By similarity
Disulfide bond237Interchain; in linked form By similarity

Experimental info

Non-terminal residue11

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Sequences

Sequence LengthMass (Da)Tools
P28376-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 6C215C4A47D4F9F2

FASTA46551,579
        10         20         30         40         50         60 
VGFKAGVKDY KLTYYTPEYV TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW 

        70         80         90        100        110        120 
TDGLTSLDRY KGRCYNIEPV AGEENQYICY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL 

       130        140        150        160        170        180 
RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY 

       190        200        210        220        230        240 
ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIFKSQA ETGEIKGHYL NATAGTCEEM 

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

       310        320        330        340        350        360 
FRVLAKALRM SGGDHIHAGT VVGKLEGERD ITLGFVDLLR DDFIEKDRSR GIYFTQDWVS 

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

       430        440        450        460 
RNEGRDLARE GNEIIREASK WSAELAAACE VWKEIKFQFE AMDTL

« Hide

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References

[1]"Carnivorous plants: phylogeny and structural evolution."
Albert V.A., Williams S.E., Chase M.W.
Science 257:1491-1495(1992) [PubMed: 1523408] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

L01881 Genomic DNA. Translation: AAA84006.2.
L13181 Genomic DNA. Translation: AAA93537.1. Different initiation.

3D structure databases

HSSPHSSP built from PDB template 3RUB based on UniProtKB P00876.
SMRP28376. Positions 1-465.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.1.39. 270413.

Family and domain databases

HAMAPMF_01338.
[Tree]
InterProIPR000685. 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]
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameRBL_ACESA
AccessionPrimary (citable) accession number: P28376
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents