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Q8PXG9 (RBL_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 lineageArchaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina ›

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Subunit structure

Homodimer By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133
PRO_0000062674

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 site991Substrate; in homodimeric partner By similarity
Binding site1531Substrate By similarity
Binding site2711Substrate By similarity
Binding site3031Substrate By similarity
Binding site3541Substrate 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...

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.

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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 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: May 1, 2013
This is version 77 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

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