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A4WZV1 (RBL2_RHOS5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Rsph17025_4063
Encoded onPlasmid pRSPA02
OrganismRhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP]
Taxonomic identifier349102 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
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. 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. HAMAP MF_01338

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. HAMAP MF_01338

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 2 HAMAP MF_01338
PRO_0000355753

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
A4WZV1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: C4D940B33CA93819

FASTA47353,109
        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 LGLSAKNYGR 

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

       250        260        270        280        290        300 
EEIYERAEFA KEIGTPIIMS DYLTVGWSAH 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 CANRFALEAC 

       430        440        450        460        470 
VQARNDGRNL EKEGKEILTK AAQTSPELRM AMETWKEVRF EFDTVDKLDV QHR

« Hide

References

[1]"Complete sequence of plasmid pRSPA02 of Rhodobacter sphaeroides ATCC 17025."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17025 / ATH 2.4.3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000663 Genomic DNA. Translation: ABP72915.1.
RefSeqYP_001170220.1. NC_009430.1.

3D structure databases

ProteinModelPortalA4WZV1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4WZV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5086236.
GenomeReviewsGene locus Rsph17025_4063 in contig CP000663_GR.
KEGGrsq:Rsph17025_4063.
PATRIC23166660. VBIRhoSph94549_4206.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHBG405441.
OMAEYRETYW.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycRSPH349102:RSPH17025_4063-MONOMER.

Family and domain databases

HAMAPMF_01338. RuBisCO_L_type1.
[Tree]
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. 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.
KOK01601.
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL2_RHOS5
AccessionPrimary (citable) accession number: A4WZV1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 34 of the entry and version 1 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

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