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Reviewed, UniProtKB/Swiss-Prot P22859 (RBL1B_CHRVI)

Last modified March 24, 2009. Version 66. 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 2
      Short name=RuBisCO large subunit 2
    EC=4.1.1.39
Gene names
Name: cbbL2
Synonyms: rbcL
OrganismChromatium vinosum (Allochromatium vinosum)
Taxonomic identifier1049 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Both reactions occur simultaneously and in competition at the same active site. 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.

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.

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.

Caution

In C.vinosum two similar set of genes code for RuBisCO large and small chains: the rbcL-rbcS and the rbcA-rbcB sets. Under standard photoautotrophic culture conditions only the latter set seems active, the former probably being cryptic.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 471470Ribulose bisphosphate carboxylase large chain 2 HAMAP MF_01338
PRO_0000062622

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
Disulfide bond240Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
P22859-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FB79F09C6C33B885

FASTA47152,394
        10         20         30         40         50         60 
MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL FEEGSIVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRALRLED IRFPLHYVKT CGGPRNGIQV ERDRMDKYGR PFLGATVKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYEMLRGGL DFTKDDENVN SQPFMRWQNR FEFVSEAVRK AREETGERKG HYLNVTAPTC 

       250        260        270        280        290        300 
EEMFKRAEFA KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRHPKH 

       310        320        330        340        350        360 
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED RSRGLFFDQD 

       370        380        390        400        410        420 
WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ GHPWGNAAGA AANRVATEAC 

       430        440        450        460        470 
VKARNEGVEI EKHAREVLSD AARHSPELAV AMETWKEIKF EFDVVDKLDA A 

« Hide

References

[1]"Sequence and expression of genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum."
Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K., Shinozaki K., Kobayashi K., Sugiura M.
Gene 97:55-62(1991) [PubMed: 1899846] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 17899 / DSM 180 / D.
[2]"Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum."
Viale A.M., Kobayashi H., Akazawa T.
J. Biol. Chem. 265:18386-18392(1990) [PubMed: 2211708] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.

Cross-references

Sequence databases

D90204 Genomic DNA. Translation: BAA14229.1.
PIRRKKRL2. JQ0586.

3D structure databases

HSSPHSSP built from PDB template 1GEH based on UniProtKB O93627.
SMRP22859. Positions 5-467, 6-468.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.1.39. 2799.

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 nameRBL1B_CHRVI
AccessionPrimary (citable) accession number: P22859
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: March 24, 2009
This is version 66 of the entry and version 3 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