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

A4YNR1 (RBL1A_BRASO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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 1

Short name=RuBisCO large subunit 1
EC=4.1.1.39
Gene names
Name:cbbL1
Ordered Locus Names:BRADO1659
OrganismBradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]
Taxonomic identifier114615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length486 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 – 486486Ribulose bisphosphate carboxylase large chain 1 HAMAP-Rule MF_01338
PRO_0000299961

Sites

Active site1771Proton acceptor By similarity
Active site2951Proton acceptor By similarity
Metal binding2031Magnesium; via carbamate group By similarity
Metal binding2051Magnesium By similarity
Metal binding2061Magnesium By similarity
Binding site1251Substrate; in homodimeric partner By similarity
Binding site1751Substrate By similarity
Binding site1791Substrate By similarity
Binding site2961Substrate By similarity
Binding site3281Substrate By similarity
Binding site3801Substrate By similarity
Site3351Transition state stabilizer By similarity

Amino acid modifications

Modified residue2031N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YNR1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: D969770506D00683

FASTA48653,965
        10         20         30         40         50         60 
MNDQSITVRG KDRYKSGVME YKKMGYWEPS YQPNDTDVIA LFRVTPQDGV DPVEACAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTAAE KYRAKCYRVE PVPGSPGSYF AYIAYDLDLF EPGSIANLTA 

       130        140        150        160        170        180 
SIIGNVFGFK PLKALRLEDM RLPVAYVKTF QGPATGIVVE RERLDKFGRP LLGATVKPKL 

       190        200        210        220        230        240 
GLSGRNYGRV VYEALKGGLD FTKDDENINS QPFMHWRERF LYCMEAVNKA QAATGEIKGT 

       250        260        270        280        290        300 
YLNVTAATME DMYERAEFAK ELGSNIIMID LVIGYTAIQS MAKWSRKNDM ILHLHRAGHS 

       310        320        330        340        350        360 
TYTRQRAHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDIC REDFNPMRLE 

       370        380        390        400        410        420 
HGVFFDQHWA SLNKLMPVAS GGIHAGQMHQ LLDLLGEDVV LQFGGGTIGH PRGIAAGATA 

       430        440        450        460        470        480 
NRVALEAMIL ARNEGRDYVH EGPEILAKAA MTCTPLREAL EIWKDVTFNY ESTDSPDFVP 


TVTPAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU234118 Genomic DNA. Translation: CAL75537.1.
RefSeqYP_001203774.1. NC_009445.1.

3D structure databases

ProteinModelPortalA4YNR1.
SMRA4YNR1. Positions 13-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING114615.BRADO1659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL75537; CAL75537; BRADO1659.
GeneID5115881.
KEGGbra:BRADO1659.
PATRIC21219543. VBIBraSp122330_1596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMALDYYLEC.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycBSP114615:GJN5-1579-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 nameRBL1A_BRASO
AccessionPrimary (citable) accession number: A4YNR1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 45 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