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Q8THG2 (RBL_METAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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:MA_4555
OrganismMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) [Reference proteome] [HAMAP]
Taxonomic identifier188937 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Enzyme regulation

Reversibly inhibited by O2. HAMAP-Rule MF_01133

Subunit structure

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

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.

Biophysicochemical properties

Temperature dependence:

Active from 25 to 40 degrees Celsius. HAMAP-Rule MF_01133

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133
PRO_0000062672

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
Q8THG2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B03BFCBD9E8AFED5

FASTA42846,787
        10         20         30         40         50         60 
MRRDYVDPGY SPKDTDLICE FHIEPAAGIS FEEASTHMAG ESSIDSWTEI STLSPELAAR 

        70         80         90        100        110        120 
LKPHVFYLDA DTQTVRVAYS EDLFELGSVP QVLSAVAGNI FSMKIVDNLR LQDITFPKSM 

       130        140        150        160        170        180 
LREFEGPNFG LPGVRDIVGV KDRPLVGTIV KPKVGLTSEM HAEVAYNAFA GGCDLVKDDE 

       190        200        210        220        230        240 
NLTDQKFNGF EKRAELTLKI AEKAEAETGE RKMYLCNITA PTCEEMIRRL HVLKDLGASY 

       250        260        270        280        290        300 
AMIDIVPTGW TALQTLREAA ADEGLALHAH RCMHSAFTRN PRHGVSMLLV AKLCRLIGLD 

       310        320        330        340        350        360 
QLHIGTVVGK MHGDKDEVLS IRDECVLDTV PADPEQHVLA QDWGGLKPMF PVASGGLAPT 

       370        380        390        400        410        420 
MIPDLYSIFG KEVIMQFGGG IHAHPMGTAA GAAACRQALE ASLEGISLQD YAKDHKELEA 


ALGKWLEK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010299 Genomic DNA. Translation: AAM07894.1.
RefSeqNP_619414.1. NC_003552.1.

3D structure databases

ProteinModelPortalQ8THG2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING188937.MA4555.

Proteomic databases

PRIDEQ8THG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM07894; AAM07894; MA_4555.
GeneID1476449.
KEGGmac:MA4555.

Phylogenomic databases

eggNOGCOG1850.
KOK01601.
OMAHRAMHAA.
PhylomeDBQ8THG2.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycMACE188937:GI2O-4613-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_METAC
AccessionPrimary (citable) accession number: Q8THG2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 84 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