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P22859 (RBL1B_ALLVD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2

Short name=RuBisCO large subunit 2
EC=4.1.1.39
Gene names
Name:cbbL2
Synonyms:rbcL
Ordered Locus Names:Alvin_2750
OrganismAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum) [Complete proteome] [HAMAP]
Taxonomic identifier572477 [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-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; 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. 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.

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.3
Chain2 – 471470Ribulose bisphosphate carboxylase large chain 2 HAMAP-Rule 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

Experimental info

Sequence conflict1451P → R in BAA14229. Ref.1
Sequence conflict2221Q → R in BAA14229. Ref.1
Sequence conflict2971N → H in BAA14229. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22859 [UniParc].

Last modified June 15, 2010. Version 4.
Checksum: 08A26940B6458D97

FASTA47152,284
        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 CGGPPNGIQV ERDRMDKYGR PFLGATVKPK LGLSAKNYGR 

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

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

       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

« Hide 'large scale' 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome of Allochromatium vinosum DSM 180."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D.
[3]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90204 Genomic DNA. Translation: BAA14229.1.
CP001896 Genomic DNA. Translation: ADC63659.1.
PIRRKKRL2. JQ0586.
RefSeqYP_003444691.1. NC_013851.1.

3D structure databases

ProteinModelPortalP22859.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADC63659; ADC63659; Alvin_2750.
GeneID8788139.
KEGGalv:Alvin_2750.
PATRIC31925280. VBIAllVin64954_2712.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycAVIN572477:GCJK-2812-MONOMER.

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 nameRBL1B_ALLVD
AccessionPrimary (citable) accession number: P22859
Secondary accession number(s): D3RQ48
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 15, 2010
Last modified: February 19, 2014
This is version 91 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families