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Q8PXG9 (RBL_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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:MM_1249
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [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_0000062674

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
Q8PXG9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 89262149EDB15A12

FASTA42847,138
        10         20         30         40         50         60 
MRRDYIDIGY SPKETDLVCE FHIEPTAGVN FEEAATHLAG ESSIDSWTEI ATLSPELAEK 

        70         80         90        100        110        120 
LKPHVFYADE GAQTVRVAYS EELFELGSVP QVLSAVAGNI LSMKIVDNVR LQDIAFPKSM 

       130        140        150        160        170        180 
INEFKGPNFG LPGIRKLVGV QDRPLIGTIV KPKVGLNSEK HAEVAYNSFV GGCDLVKDDE 

       190        200        210        220        230        240 
NLSDQKFNSF EKRAELTLKL AEKAESETGE KKMYLCNVTA PTCREMIRRM NFLKDLGASY 

       250        260        270        280        290        300 
VMVDIVPAGW TAIQTLREEA EDAGLALHAH RCMHSAYTRN PRHGISMLVV AKLCRLIGLD 

       310        320        330        340        350        360 
QLHIGTVVGK MHGEKHEVLN LRDQCVLDKV PADESQHILA QDWRGLKPMF PVASGGLAPT 

       370        380        390        400        410        420 
MIPDLYSIFG KDVIMQFGGG IHAHPMGTVA GATACRQALE ASLEGISLQD YAKNHKELET 


ALGKWLKK 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM30945.1.
RefSeqNP_633273.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PXG9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192952.MM_1249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM30945; AAM30945; MM_1249.
GeneID1479591.
KEGGmma:MM_1249.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycMMAZ192952:GCK2-1279-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_METMA
AccessionPrimary (citable) accession number: Q8PXG9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 81 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