Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A4YQD3 (RBL1B_BRASO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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
Ordered Locus Names:BRADO2274
OrganismBradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]
Taxonomic identifier114615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length479 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-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.

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 – 479479Ribulose bisphosphate carboxylase large chain 2 HAMAP-Rule MF_01338
PRO_0000299962

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
A4YQD3 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 7518D7CC0AE30D6C

FASTA47953,334
        10         20         30         40         50         60 
MAEKSYQAGV KEYRKTYWTP EYVPLDTDLL AVFKIVAQAG VPREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYRI EPVPGDDNAF YAFIAYPIDL FEEGSVVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRSLRLED IRFPLAYVKT CGGPPNGIQL ERDRLNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENIN SQPFMRWQHR FEFVMEAVHK ATSETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEFA KSLGAPIIMH DFLTAGFTAN TGLANWCREN GMLLHIHRAM HAVLDRNPMH 

       310        320        330        340        350        360 
GIHFRVLTKC LRLSGGDHLH SGTVVGKLEG DREATIGWVD LMREPFVPEN RARGIFFDQD 

       370        380        390        400        410        420 
WGAMPGVMPV ASGGIHVWHM PALTAIFGDD ACFQFGGGTL GHPWGNAAGA HANRVALEAC 

       430        440        450        460        470 
VEARNQGRPV EREGREILTE AAQHSPELKI AMETWKEIKF EFDVVDKLDT GPMLRVVNA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU234118 Genomic DNA. Translation: CAL76109.1.
RefSeqYP_001204346.1. NC_009445.1.

3D structure databases

ProteinModelPortalA4YQD3.
SMRA4YQD3. Positions 16-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING114615.BRADO2274.

Proteomic databases

PRIDEA4YQD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL76109; CAL76109; BRADO2274.
GeneID5115889.
KEGGbra:BRADO2274.
PATRIC21220737. VBIBraSp122330_2191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAMSIFKGV.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycBSP114615:GJN5-2154-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_BRASO
AccessionPrimary (citable) accession number: A4YQD3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 44 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