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Q58632 (RBL_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:rbcL
Ordered Locus Names:MJ1235
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the addition of molecular CO2 and H2O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase By similarity. HAMAP-Rule MF_01133

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01133

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01133

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01133

Enzyme regulation

Reversibly inhibited by O2. HAMAP-Rule MF_01133

Subunit structure

Homodimer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.

Miscellaneous

Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O2 to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains (PubMed:17303759).

Sequence similarities

Belongs to the RuBisCO large chain family. Type III subfamily.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 65 degrees Celsius. Highly thermostable. HAMAP-Rule MF_01133

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133
PRO_0000062673

Regions

Region353 – 3553Substrate binding By similarity
Region375 – 3784Substrate binding By similarity

Sites

Active site1531Proton acceptor By similarity
Active site2691Proton acceptor By similarity
Metal binding1791Magnesium; via carbamate group By similarity
Metal binding1811Magnesium By similarity
Metal binding1821Magnesium By similarity
Binding site1551Substrate By similarity
Binding site2701Substrate By similarity
Binding site3021Substrate By similarity
Site3091Transition state stabilizer By similarity

Amino acid modifications

Modified residue1791N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q58632 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: C6F9F1653BA76039

FASTA42547,859
        10         20         30         40         50         60 
MDYINLNYRP NEGDLLSCMV IKGENLEKLA NEIAGESSIG TWTKVQTMKS DIYEKLRPKV 

        70         80         90        100        110        120 
YEIKEIGEEN GYKVGLIKIA YPLYDFEINN MPGVLAGIAG NIFGMKIAKG LRILDFRFPA 

       130        140        150        160        170        180 
EFVKAYKGPR FGIEGVRETL KIKERPLLGT IVKPKVGLKT EEHAKVAYEA WVGGVDLVKD 

       190        200        210        220        230        240 
DENLTSQEFN KFEDRIYKTL EMRDKAEEET GERKAYMPNI TAPYREMIRR AEIAEDAGSE 

       250        260        270        280        290        300 
YVMIDVVVCG FSAVQSFREE DFKFIIHAHR AMHAAMTRSR DFGISMLALA KIYRLLGVDQ 

       310        320        330        340        350        360 
LHIGTVVGKM EGGEKEVKAI RDEIVYDKVE ADNENKFFNQ DWFDIKPVFP VSSGGVHPRL 

       370        380        390        400        410        420 
VPKIVEILGR DLIIQAGGGV HGHPDGTRAG AKAMRAAIEA IIEGKSLEEK AEEVAELKKA 


LEYWK 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99239.1.
RefSeqNP_248230.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58632.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99239; AAB99239; MJ_1235.
GeneID1452131.
KEGGmja:MJ_1235.

Phylogenomic databases

eggNOGCOG1850.
KOK01601.
OMAHRAMHAA.
ProtClustDBPRK04208.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01133. RuBisCO_L_type3.
InterProIPR017712. RuBisCO_III.
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.
TIGRFAMsTIGR03326. rubisco_III. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRBL_METJA
AccessionPrimary (citable) accession number: Q58632
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 1998
Last modified: February 19, 2014
This is version 94 of the entry and version 2 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names