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D3S3X8 (D3S3X8_METSF) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase HAMAP-Rule MF_01133

Short name=RuBisCO HAMAP-Rule MF_01133
EC=4.1.1.39 HAMAP-Rule MF_01133
Gene names
Name:rbcL HAMAP-Rule MF_01133
Ordered Locus Names:MFS40622_0859 EMBL ADC69542.1
OrganismMethanocaldococcus sp. (strain FS406-22) [Complete proteome] [HAMAP] EMBL ADC69542.1
Taxonomic identifier644281 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length425 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. HAMAP-Rule MF_01133

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) By similarity. HAMAP-Rule MF_01133

Sequence similarities

Belongs to the RuBisCO large chain family. Type III subfamily. HAMAP-Rule MF_01133

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region353 – 3553Substrate binding By similarity HAMAP-Rule MF_01133
Region375 – 3784Substrate binding By similarity HAMAP-Rule MF_01133

Sites

Active site1531Proton acceptor By similarity HAMAP-Rule MF_01133
Active site2691Proton acceptor By similarity HAMAP-Rule MF_01133
Metal binding1791Magnesium; via carbamate group By similarity HAMAP-Rule MF_01133
Metal binding1811Magnesium By similarity HAMAP-Rule MF_01133
Metal binding1821Magnesium By similarity HAMAP-Rule MF_01133
Binding site1551Substrate By similarity HAMAP-Rule MF_01133
Binding site2701Substrate By similarity HAMAP-Rule MF_01133
Binding site3021Substrate By similarity HAMAP-Rule MF_01133
Site3091Transition state stabilizer By similarity HAMAP-Rule MF_01133

Amino acid modifications

Modified residue1791N6-carboxylysine By similarity HAMAP-Rule MF_01133

Sequences

Sequence LengthMass (Da)Tools
D3S3X8 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: B582FABD358CCCCA

FASTA42547,959
        10         20         30         40         50         60 
MDYINLNYTP NENDLLSCMI IKGENLEKLA NEIAGESSIG TWTKVQTMKS DIYEKLRPKV 

        70         80         90        100        110        120 
YEIKEIGNDG KYKVGLIKIA YPLYDFEINN MPGVLAGIAG NIFGMKIAKG LRILDFRFPE 

       130        140        150        160        170        180 
EFVKAYKGPR FGIEGVRETL KIKERPLLGT IVKPKVGLKT EEHAKVAYEA WVGGVDLVKD 

       190        200        210        220        230        240 
DENLTSQEFN KFEDRIYKTL EMRDKAEEET GERKAYMPNI TAPYREMIRR VEIAEDAGSE 

       250        260        270        280        290        300 
YVMIDVVVCG FSAVQSFREE EFKFIIHAHR AMHAAMTRSR DFGISMLVLA KIYRLLGVDQ 

       310        320        330        340        350        360 
LHIGTVVGKM EGGEKEVKSI RDEIVCDKVE ADDENKFFNQ EWFDIKPVFP VSSGGVHPRL 

       370        380        390        400        410        420 
VPKIVEILGR DLIIQAGGGV HGHPDGTRAG AKAMRAAIEA IIEGKSLEEK AEEVAELKKA 


LEYWK 

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References

[1]"Complete sequence of chromosome of Methanocaldococcus sp. FS406-22."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Leigh J., Whitman W.B., Woyke T.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FS406-22 EMBL ADC69542.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001901 Genomic DNA. Translation: ADC69542.1.
RefSeqYP_003458278.1. NC_013887.1.

3D structure databases

ProteinModelPortalD3S3X8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADC69542; ADC69542; MFS40622_0859.
GeneID8804702.
KEGGmfs:MFS40622_0859.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
OMAHRAMHAA.

Enzyme and pathway databases

BioCycMSP644281:GI4H-868-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 nameD3S3X8_METSF
AccessionPrimary (citable) accession number: D3S3X8
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: February 19, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)