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A5GS63 (RBL_SYNR3) 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
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Synonyms:rbcL
Ordered Locus Names:SynRCC307_0819
OrganismSynechococcus sp. (strain RCC307) [Complete proteome] [HAMAP]
Taxonomic identifier316278 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length471 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 in the photorespiration process. 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 – 471471Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_1000067648

Sites

Active site1671Proton acceptor By similarity
Active site2861Proton acceptor By similarity
Metal binding1931Magnesium; via carbamate group By similarity
Metal binding1951Magnesium By similarity
Metal binding1961Magnesium By similarity
Binding site1151Substrate; in homodimeric partner By similarity
Binding site1651Substrate By similarity
Binding site1691Substrate By similarity
Binding site2871Substrate By similarity
Binding site3191Substrate By similarity
Binding site3711Substrate By similarity
Site3261Transition state stabilizer By similarity

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GS63 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: BCEF204C77223EE5

FASTA47152,772
        10         20         30         40         50         60 
MSKKYDAGVK EYRDTYWTPD YVPLDTDLLA CFKCTGQEGV PKEEVAAAVA AESSTGTWST 

        70         80         90        100        110        120 
VWSELLTDLD FYKGRCYRIE DVPGDKESFY AFIAYPLDLF EEGSITNVLT SLVGNVFGFK 

       130        140        150        160        170        180 
ALRHLRLEDI RFPLAFIKTC YGPPNGIVVE RDRMNKYGRP LLGCTIKPKL GLSGKNYGRV 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENINS QPFQRWQNRF EFVAEAIRLA EQETGEKKGH YLNVTANTPE 

       250        260        270        280        290        300 
EMYERAEFAK ELGMPIVMHD FITGGFTANT GLSKWCRKNG MLLHIHRAMH AVIDRHPKHG 

       310        320        330        340        350        360 
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDQ LRESFVPEDR SRGNFFDQDW 

       370        380        390        400        410        420 
GSMPGVFAVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTHG HPWGSAAGAA ANRVALEACV 

       430        440        450        460        470 
KARNAGRHLE KESRDILMEA AKHSPELAIA LETWKEIKFE FDTVDKLDVQ S 

« Hide

References

[1]Genoscope
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCC307.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT978603 Genomic DNA. Translation: CAK27722.1.
RefSeqYP_001227075.1. NC_009482.1.

3D structure databases

ProteinModelPortalA5GS63.
SMRA5GS63. Positions 15-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316278.SynRCC307_0819.

Proteomic databases

PRIDEA5GS63.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK27722; CAK27722; SynRCC307_0819.
GeneID5158598.
KEGGsyr:SynRCC307_0819.
PATRIC23822510. VBISynSp108374_0812.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.

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 nameRBL_SYNR3
AccessionPrimary (citable) accession number: A5GS63
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 12, 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