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Q46E16 (RBL_METBF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:Mbar_A0902
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Subunit structure

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

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.

Ontologies

Keywords
   Biological processCarbon dioxide fixation
   LigandMagnesium
Metal-binding
   Molecular functionLyase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processAMP catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

carbon fixation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribulose-bisphosphate carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133
PRO_1000065430

Regions

Region354 – 3563Substrate binding By similarity
Region376 – 3794Substrate binding By similarity

Sites

Active site1511Proton acceptor By similarity
Active site2701Proton acceptor By similarity
Metal binding1771Magnesium; via carbamate group By similarity
Metal binding1791Magnesium By similarity
Metal binding1801Magnesium By similarity
Binding site1531Substrate By similarity
Binding site2711Substrate By similarity
Binding site3031Substrate By similarity
Site3101Transition state stabilizer By similarity

Amino acid modifications

Modified residue1771N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46E16 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 74DCE0F7F03502E3

FASTA42847,061
        10         20         30         40         50         60 
MQRDYIDAGY SPKDTDLICE FHIEPSAGVN FEEAATHMAG ESSIDSWTEI ATLSPELAAR 

        70         80         90        100        110        120 
LKPHVFYMDE DAQTVRVAYS EELFELGSVP QVLSAVAGNI LSMKIVDNLR LQDIAFPKSM 

       130        140        150        160        170        180 
LREFKGPGFG LSGIRELTGV QDRPLIGTIV KPKVGLTSEK HAEVAYNSFA GGCDLVKDDE 

       190        200        210        220        230        240 
NLTDQKFNKF EKRAELTLKL AEKAESETGE RKMYLCNITA PTCKEMIRRM NILKDLGASY 

       250        260        270        280        290        300 
AMIDIVPAGW TALQTLREEA DDAGLALHAH RCMHSAYTRN PRHGISMLVV AKLCRLIGLD 

       310        320        330        340        350        360 
QLHIGTVVGK MHGEKHEVLS LRDECVLDNV PADESQHVLA QDWGGLKPMF PVASGGLAPT 

       370        380        390        400        410        420 
MIPDLYTIFG RDVIMQFGGG IHAHPMGTKA GAAACRQALE ASLEGVSLQE YAKNHRELEA 


AINKWLKK 

« Hide

References

[1]"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fusaro / DSM 804.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000099 Genomic DNA. Translation: AAZ69876.1.
RefSeqYP_304456.1. NC_007355.1.

3D structure databases

ProteinModelPortalQ46E16.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269797.Mbar_A0902.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ69876; AAZ69876; Mbar_A0902.
GeneID3625947.
KEGGmba:Mbar_A0902.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycMBAR269797:GHUW-916-MONOMER.

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_METBF
AccessionPrimary (citable) accession number: Q46E16
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 61 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