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Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation1 Publication
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Enzyme regulationi

Reversibly inhibited by O2.2 Publications

Temperature dependencei

Optimum temperature is 65 degrees Celsius. Highly thermostable.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531Proton acceptorUniRule annotation
Binding sitei155 – 1551SubstrateUniRule annotation
Metal bindingi179 – 1791Magnesium; via carbamate groupUniRule annotation
Metal bindingi181 – 1811MagnesiumUniRule annotation
Metal bindingi182 – 1821MagnesiumUniRule annotation
Active sitei269 – 2691Proton acceptorUniRule annotation
Binding sitei270 – 2701SubstrateUniRule annotation
Binding sitei302 – 3021SubstrateUniRule annotation
Sitei309 – 3091Transition state stabilizerUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.1.1.39. 3260.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:rbcLUniRule annotation
Ordered Locus Names:MJ1235
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
ProteomesiUP000000805 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Ribulose bisphosphate carboxylasePRO_0000062673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits.2 Publications

Protein-protein interaction databases

STRINGi243232.MJ1235.

Structurei

3D structure databases

ProteinModelPortaliQ58632.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni353 – 3553Substrate bindingUniRule annotation
Regioni375 – 3784Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
InParanoidiQ58632.
KOiK01601.
OMAiHAAFTRN.
PhylomeDBiQ58632.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01133. RuBisCO_L_type3.
InterProiIPR017712. RuBisCO_III.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsiTIGR03326. rubisco_III. 1 hit.

Sequencei

Sequence statusi: Complete.

Q58632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYINLNYRP NEGDLLSCMV IKGENLEKLA NEIAGESSIG TWTKVQTMKS
60 70 80 90 100
DIYEKLRPKV YEIKEIGEEN GYKVGLIKIA YPLYDFEINN MPGVLAGIAG
110 120 130 140 150
NIFGMKIAKG LRILDFRFPA EFVKAYKGPR FGIEGVRETL KIKERPLLGT
160 170 180 190 200
IVKPKVGLKT EEHAKVAYEA WVGGVDLVKD DENLTSQEFN KFEDRIYKTL
210 220 230 240 250
EMRDKAEEET GERKAYMPNI TAPYREMIRR AEIAEDAGSE YVMIDVVVCG
260 270 280 290 300
FSAVQSFREE DFKFIIHAHR AMHAAMTRSR DFGISMLALA KIYRLLGVDQ
310 320 330 340 350
LHIGTVVGKM EGGEKEVKAI RDEIVYDKVE ADNENKFFNQ DWFDIKPVFP
360 370 380 390 400
VSSGGVHPRL VPKIVEILGR DLIIQAGGGV HGHPDGTRAG AKAMRAAIEA
410 420
IIEGKSLEEK AEEVAELKKA LEYWK
Length:425
Mass (Da):47,859
Last modified:June 1, 1998 - v2
Checksum:iC6F9F1653BA76039
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99239.1.
RefSeqiNP_248230.1. NC_000909.1.
WP_010870747.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB99239; AAB99239; MJ_1235.
GeneIDi1452131.
KEGGimja:MJ_1235.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99239.1.
RefSeqiNP_248230.1. NC_000909.1.
WP_010870747.1. NC_000909.1.

3D structure databases

ProteinModelPortaliQ58632.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ1235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99239; AAB99239; MJ_1235.
GeneIDi1452131.
KEGGimja:MJ_1235.

Phylogenomic databases

eggNOGiCOG1850.
InParanoidiQ58632.
KOiK01601.
OMAiHAAFTRN.
PhylomeDBiQ58632.

Enzyme and pathway databases

BRENDAi4.1.1.39. 3260.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01133. RuBisCO_L_type3.
InterProiIPR017712. RuBisCO_III.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsiTIGR03326. rubisco_III. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. "Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic Archaea."
    Watson G.M.F., Yu J.-P., Tabita F.R.
    J. Bacteriol. 181:1569-1575(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  3. "Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea."
    Finn M.W., Tabita F.R.
    J. Bacteriol. 185:3049-3059(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Entry informationi

Entry nameiRBL_METJA
AccessioniPrimary (citable) accession number: Q58632
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 1998
Last modified: May 27, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.