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P23755 (RBL_GALSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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
Encoded onPlastid; Chloroplast
OrganismGaldieria sulphuraria (Red alga)
Taxonomic identifier130081 [NCBI]
Taxonomic lineageEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeGaldieria

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
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 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 By similarity.

Subcellular location

Plastidchloroplast 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.

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062476

Sites

Active site1841Proton acceptor By similarity
Active site3021Proton acceptor By similarity
Metal binding2101Magnesium; via carbamate group By similarity
Metal binding2121Magnesium By similarity
Metal binding2131Magnesium By similarity
Binding site1321Substrate; in homodimeric partner By similarity
Binding site1821Substrate By similarity
Binding site1861Substrate By similarity
Binding site3031Substrate By similarity
Binding site3351Substrate By similarity
Binding site3871Substrate By similarity
Site3421Transition state stabilizer By similarity

Amino acid modifications

Modified residue2101N6-carboxylysine By similarity

Secondary structure

................................................................................. 493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23755 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: B69EE280D47C6FA2

FASTA49354,989
        10         20         30         40         50         60 
MSQSLEEKSV QERTRIKNSR YESGVIPYAK MGYWNPDYQV KDTDVLALFR VTPQPGVDPI 

        70         80         90        100        110        120 
EAAAAVAGES STATWTVVWT DLLTAADLYR AKAYKVDQVP NNPEQYFAYI AYELDLFEEG 

       130        140        150        160        170        180 
SIANLTASII GNVFGFKAVK ALRLEDMRLP FAYIKTFQGP ATGVILERER LDKFGRPLLG 

       190        200        210        220        230        240 
CTTKPKLGLS GKNYGRVVYE ALKGGLDFVK DDENINSQPF MRWRERYLFV MEAVNKAAAA 

       250        260        270        280        290        300 
TGEVKGHYLN VTAATMEEMY ARAQLAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH 

       310        320        330        340        350        360 
LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT RGFYKTLLLP 

       370        380        390        400        410        420 
KLERNLQEGL FFDMDWASLR KVMPVASGGI HAGQMHQLIH YLGEDVVLQF GGGTIGHPDG 

       430        440        450        460        470        480 
IQSGATANRV ALEAMILARN ENRDFLTEGP EILREAAKNC GALRTALDLW KDITFNYTST 

       490 
DTSDFVETPT ANI 

« Hide

References

[1]"Structure of the Rubisco operon from the unicellular red alga Cyanidium caldarium: evidence for a polyphyletic origin of the plastids."
Valentin K.-U., Zetsche K.
Mol. Gen. Genet. 222:425-430(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 14-1-1 / Isolate 107.79/Goettingen.
[2]Whitney S.M., Andrews J.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: UTEX 2393.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55524 Genomic DNA. Translation: CAA39140.1.
AF233069 Genomic DNA. Translation: AAF81681.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F0HX-ray1.96A1-493[»]
4F0KX-ray2.05A1-493[»]
4F0MX-ray2.25A1-493[»]
ProteinModelPortalP23755.
SMRP23755. Positions 14-486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60089N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL_GALSU
AccessionPrimary (citable) accession number: P23755
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: February 19, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references