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Reviewed, UniProtKB/Swiss-Prot O32740 (RBL1_RHOCA)

Last modified March 24, 2009. Version 51. 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

Names and origin

Protein namesRecommended name:
    Ribulose bisphosphate carboxylase large chain
      Short name=RuBisCO large subunit
    EC=4.1.1.39
Gene names
Name: cbbL
Synonyms: cbbL1
OrganismRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifier1061 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Ribulose bisphosphate carboxylase large chain HAMAP MF_01338
PRO_0000062645

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 residue1941N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O32740-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9F2C3173618B9958

FASTA47353,037
        10         20         30         40         50         60 
MAAKTYDAGV KDYRSIYWEP QYQVKDSDIL AVFKVVPQPG VSREEAAAAV AAESSTATWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYAI EDVPGSDEAF YAFIAYPMDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRALRLED VRFPLWFVMT CPGAPHGMKV ERDLLDKYGR PLLGCTIKPK LGLAAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENVN SQPFLRWRDR FLFCQEAIQK AEAETGERKG HYMNVTAGTM 

       250        260        270        280        290        300 
EEIYERAEFA KEIGTPIIMS DYLTVGWAAH TSLSRWCRKN GMLLHVHRAM HAVMDRNPNH 

       310        320        330        340        350        360 
GINFRVLAKI LRLMGGDHLH SGTVVGKLEG DREATIGWIN LLRDRFIKAD RSRGIFFDQD 

       370        380        390        400        410        420 
WGPQPGLFPV ASGGIHVWHM PALVSIFGND SVLQFGGGTL GHPWGNAAGA CANRVALEAC 

       430        440        450        460        470 
VQARNEGRHL EKEGKEILTK AAQSSPELRM AMETWKEIKF EFDTVDKLDV QHR 

« Hide

References

[1]"Rhodobacter capsulatus genes encoding form I ribulose-1,5-bisphosphate carboxylase/oxygenase (cbbLS) and neighbouring genes were acquired by a horizontal gene transfer."
Paoli G.C., Soyer F., Shively J., Tabita F.R.
Microbiology 144:219-227(1998) [PubMed: 9467914] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Expression of the cbbLcbbS and cbbM genes and distinct organization of the cbb Calvin cycle structural genes of Rhodobacter capsulatus."
Paoli G.C., Morgan N.S., Tabita F.R., Shively J.M.
Arch. Microbiol. 164:396-405(1995) [PubMed: 8588741] [Abstract]
Cited for: OPERON ORGANIZATION.
Strain: ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis.

Cross-references

Sequence databases

L82000 Genomic DNA. Translation: AAC37141.1.

3D structure databases

HSSPHSSP built from PDB template 1GEH based on UniProtKB O93627.
SMRO32740. Positions 2-468.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.1.39. 567.

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...

Entry information

Entry nameRBL1_RHOCA
AccessionPrimary (citable) accession number: O32740
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: March 24, 2009
This is version 51 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)

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