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Reviewed, UniProtKB/Swiss-Prot P25413 (RBL_AEGCR)

Last modified June 16, 2009. Version 63. 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
OrganismAegilops crassa (Persian goatgrass) (Triticum crassum)
Taxonomic identifier4481 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Aegilops

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Protein attributes

Sequence length421 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 – 421›421Ribulose bisphosphate carboxylase large chain HAMAP MF_01338
PRO_0000062343

Sites

Active site1201Proton acceptor By similarity
Active site2391Proton acceptor By similarity
Metal binding1461Magnesium; via carbamate group By similarity
Metal binding1481Magnesium By similarity
Metal binding1491Magnesium By similarity
Binding site681Substrate; in homodimeric partner By similarity
Binding site1181Substrate By similarity
Binding site1221Substrate By similarity
Binding site2401Substrate By similarity
Binding site2721Substrate By similarity
Binding site3241Substrate By similarity
Site2791Transition state stabilizer By similarity

Amino acid modifications

Modified residue1461N6-carboxylysine By similarity
Disulfide bond192Interchain; in linked form By similarity

Experimental info

Non-terminal residue11

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Sequences

Sequence LengthMass (Da)Tools
P25413-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 7D247DEFE169CE80

FASTA42146,901
        10         20         30         40         50         60 
AVAAESSTGT WTTVWTDGLT SLDRYKGRCY HIEPVAGEDN QWICYVAYPL DLFEEGSVTN 

        70         80         90        100        110        120 
MFTSIVGNVF GFKALRALRL EDLRIPPTYS KTFQGPPHGI QVERDKLNKY GRPLLGCTIK 

       130        140        150        160        170        180 
PKLGLSAKNY GRACYECLRG GLDFTKDDEN VNSQPFMRWR DRFVFCAEAI YKSQAETGEI 

       190        200        210        220        230        240 
KGHYLNATAG TCEEMIKRAV FARELGVPIV MHDYLTGGFT ANTTLRHYCR DNGLLLHIHR 

       250        260        270        280        290        300 
AMHAVIDRQK NHGMHFRVLA KALRMSGGDH IHSGTVVGKL EGEREMTLGF VDLLRDDFIE 

       310        320        330        340        350        360 
KDRARGIFFT QDWVSMPGVI PVASGGIHVW HMPALTEIFG DDSVLQFGGG TLGHPWGNAP 

       370        380        390        400        410        420 
GAAANRVALE ACVQARNEGR DLAREGNEII RAACKWSPEL AAACEVWKAI KFEFEPVDTI 


D

« Hide

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References

[1]"Molecular analysis of the hot spot region related to length mutations in wheat chloroplast DNAs. I. Nucleotide divergence of genes and intergenic spacer regions located in the hot spot region."
Ogihara Y., Terachi T., Sasakuma T.
Genetics 129:873-884(1991) [PubMed: 1752425] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Seedling.

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Cross-references

Sequence databases

X62118 Genomic DNA. Translation: CAA44032.1.
PIRS21984.

3D structure databases

SMRP25413. Positions 6-420.
ModBaseSearch...

Organism-specific databases

GrameneP25413.

Enzyme and pathway databases

BRENDA4.1.1.39. 301628.

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_AEGCR
AccessionPrimary (citable) accession number: P25413
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 63 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