Ribulose bisphosphate carboxylase - Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

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Q58632 (RBL_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribulose bisphosphate carboxylase
Short name=RuBisCO
EC=4.1.1.39

Gene names

Name:	rbcL
Ordered Locus Names:	MJ1235

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus ›

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Miscellaneous	The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation By similarity. HAMAP-Rule MF_01133
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

Keywords
Biological process	Carbon dioxide fixation
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbon fixation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 425

425

Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133

PRO_0000062673

Sites

Active site

153

Proton acceptor By similarity

Active site

269

Proton acceptor By similarity

Metal binding

179

Magnesium; via carbamate group By similarity

Metal binding

181

Magnesium By similarity

Metal binding

182

Magnesium By similarity

Binding site

101

Substrate; in homodimeric partner By similarity

Binding site

155

Substrate By similarity

Binding site

270

Substrate By similarity

Binding site

302

Substrate By similarity

Binding site

353

Substrate By similarity

Site

309

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

179

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q58632 [UniParc].

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

425

47,859

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. Venter J.C. Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract] 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: CHARACTERIZATION. 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: CHARACTERIZATION. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L77117 Genomic DNA. Translation: AAB99239.1.
RefSeq	NP_248230.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58632.
ModBase	Search...
Protein-protein interaction databases
STRING	243232.MJ1235.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAB99239; AAB99239; MJ_1235.
GeneID	1452131.
KEGG	mja:MJ_1235.
Phylogenomic databases
eggNOG	COG1850.
KO	K01601.
OMA	HRAMHAA.
ProtClustDB	PRK04208.
Family and domain databases
Gene3D	3.20.20.110. 1 hit. 3.30.70.150. 1 hit.
HAMAP	MF_01133. RuBisCO_L_type3.
InterPro	IPR017712. RuBisCO_III. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
SUPFAM	SSF51649. RuBisCO_large. 1 hit. SSF54966. RuBisCO_large. 1 hit.
TIGRFAMs	TIGR03326. rubisco_III. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RBL_METJA

Accession

Primary (citable) accession number: Q58632

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents