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A5E993 (RBL1A_BRASB) 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
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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:BBta_0451
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length488 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 – 488488Ribulose bisphosphate carboxylase large chain 1 HAMAP-Rule MF_01338
PRO_0000299958

Sites

Active site1791Proton acceptor By similarity
Active site2971Proton acceptor By similarity
Metal binding2051Magnesium; via carbamate group By similarity
Metal binding2071Magnesium By similarity
Metal binding2081Magnesium By similarity
Binding site1271Substrate; in homodimeric partner By similarity
Binding site1771Substrate By similarity
Binding site1811Substrate By similarity
Binding site2981Substrate By similarity
Binding site3301Substrate By similarity
Binding site3821Substrate By similarity
Site3371Transition state stabilizer By similarity

Amino acid modifications

Modified residue2051N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5E993 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 04A753A5D99867E3

FASTA48854,042
        10         20         30         40         50         60 
MNEALKSLTV TGKERYKSGV LEYKRMGYWE PDYEPKDTDV IALFRVTPQN GVDPIEASAA 

        70         80         90        100        110        120 
VAGESSTATW TVVWTDRLTA AEKYRAKCYR VDPVPNTPGS YFAYIAYDLD LFEPGSIANL 

       130        140        150        160        170        180 
SASIIGNVFG FKPLKALRLE DMRFPVAYVK TFQGPATGIV VERERLDKFG RPLLGATVKP 

       190        200        210        220        230        240 
KLGLSGRNYG RVVYEALKGG LDFTKDDENT NSQPFMHWRD RFLYCMEAVN KAQAATGEVK 

       250        260        270        280        290        300 
GTYLNVTAAT MEDMYERAEF AKELGSVIIM IDLVIGYTAI QSMAKWARRN DMILHLHRAG 

       310        320        330        340        350        360 
HGTYTRQKSH GVSFRVIAKW MRLAGVDHIH AGTVVGKLEG DPNTTRGYYD ICREDHNPMA 

       370        380        390        400        410        420 
LEYGLFFEQH WASLNKLMPV ASGGIHAGQM HQLLNYLGED VVLQFGGGTI GHPLGIQAGA 

       430        440        450        460        470        480 
TANRVALEAM ILARNEGRDY VHEGPEILAK AAATCTPLKQ ALDVWKNVTF NYDSTDTPDF 


VPTAAVTA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000494 Genomic DNA. Translation: ABQ32737.1.
RefSeqYP_001236643.1. NC_009485.1.

3D structure databases

ProteinModelPortalA5E993.
SMRA5E993. Positions 15-481.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288000.BBta_0451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ32737; ABQ32737; BBta_0451.
GeneID5154513.
KEGGbbt:BBta_0451.
PATRIC21201912. VBIBraSp29847_0655.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMACTPLKQA.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycBSP288000:GJBR-438-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_BRASB
AccessionPrimary (citable) accession number: A5E993
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 12, 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