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Q58632

- RBL_METJA

UniProt

Q58632 - RBL_METJA

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Protein
Ribulose bisphosphate carboxylase
Gene
rbcL, MJ1235
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Enzyme regulationi

Reversibly inhibited by O2.UniRule annotation

Temperature dependencei

Optimum temperature is 65 degrees Celsius. Highly thermostable.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531Proton acceptor By similarity
Binding sitei155 – 1551Substrate By similarity
Metal bindingi179 – 1791Magnesium; via carbamate group By similarity
Metal bindingi181 – 1811Magnesium By similarity
Metal bindingi182 – 1821Magnesium By similarity
Active sitei269 – 2691Proton acceptor By similarity
Binding sitei270 – 2701Substrate By similarity
Binding sitei302 – 3021Substrate By similarity
Sitei309 – 3091Transition state stabilizer By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. oxidoreductase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. AMP catabolic process Source: UniProtKB-HAMAP
  2. carbon fixation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:rbcL
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: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Ribulose bisphosphate carboxylaseUniRule annotation
PRO_0000062673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-carboxylysine By similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi243232.MJ1235.

Structurei

3D structure databases

ProteinModelPortaliQ58632.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni353 – 3553Substrate binding By similarity
Regioni375 – 3784Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
KOiK01601.
OMAiFTQDWAS.
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

MDYINLNYRP NEGDLLSCMV IKGENLEKLA NEIAGESSIG TWTKVQTMKS    50
DIYEKLRPKV YEIKEIGEEN GYKVGLIKIA YPLYDFEINN MPGVLAGIAG 100
NIFGMKIAKG LRILDFRFPA EFVKAYKGPR FGIEGVRETL KIKERPLLGT 150
IVKPKVGLKT EEHAKVAYEA WVGGVDLVKD DENLTSQEFN KFEDRIYKTL 200
EMRDKAEEET GERKAYMPNI TAPYREMIRR AEIAEDAGSE YVMIDVVVCG 250
FSAVQSFREE DFKFIIHAHR AMHAAMTRSR DFGISMLALA KIYRLLGVDQ 300
LHIGTVVGKM EGGEKEVKAI RDEIVYDKVE ADNENKFFNQ DWFDIKPVFP 350
VSSGGVHPRL VPKIVEILGR DLIIQAGGGV HGHPDGTRAG AKAMRAAIEA 400
IIEGKSLEEK AEEVAELKKA LEYWK 425
Length:425
Mass (Da):47,859
Last modified:June 1, 1998 - v2
Checksum:iC6F9F1653BA76039
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB99239.1.
RefSeqiNP_248230.1. NC_000909.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB99239.1 .
RefSeqi NP_248230.1. NC_000909.1.

3D structure databases

ProteinModelPortali Q58632.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243232.MJ1235.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB99239 ; AAB99239 ; MJ_1235 .
GeneIDi 1452131.
KEGGi mja:MJ_1235.

Phylogenomic databases

eggNOGi COG1850.
KOi K01601.
OMAi FTQDWAS.
PhylomeDBi Q58632.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01133. RuBisCO_L_type3.
InterProi IPR017712. RuBisCO_III.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
TIGRFAMsi TIGR03326. rubisco_III. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 97 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 By similarity.

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