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C7P995 (C7P995_METFA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

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
C7P995 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 0CC57F4A783A5602

FASTA42547,698
        10         20         30         40         50         60 
MDYIDLNYTP NENDLLSCMI IKGENLEKLA NEIAGESSIG TWTKVQTMKS DIYTKLKPKV 

        70         80         90        100        110        120 
YEIKEIGNEG RYKIGLIKIA YPLYAFEINN MPGVLAGIAG NIFGMKIAKG LRILDFRFPE 

       130        140        150        160        170        180 
EFVKSYKGPR FGIEGVRKTL KIKERPLLGT IVKPKVGLRT EEHAKVAYEA WVGGVDLVKD 

       190        200        210        220        230        240 
DENLTSQEFN KFEDRVYKTL EMRDKAEEET GERKAYMPNI TAPYREMLRR AEIAEDAGSE 

       250        260        270        280        290        300 
YVMIDVVVSG FSAVQSFREE EFNFIIHAHR AMHAAITRGR DFGISMLALA KIYRLLGVDQ 

       310        320        330        340        350        360 
LHIGTVVGKM EGGEKEVKAI RDEIVYDKVE ADNENKFFNQ EWFGINPIFP VSSGGVHPKL 

       370        380        390        400        410        420 
VPKIVEILGR DLIIQAGGGV HGHPDGTKAG AKAMRAAIEA VVEGKSLEEK AEEVEELKKA 


LGYWK 

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References

[1]"Complete sequence of chromosome of Methanocaldococcus fervens AG86."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Lupa-Sieprawska M., Whitman W.B.
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 4213 / JCM 157852 / AG86.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001696 Genomic DNA. Translation: ACV25127.1.
RefSeqYP_003128627.1. NC_013156.1.

3D structure databases

ProteinModelPortalC7P995.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING573064.Mefer_1318.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACV25127; ACV25127; Mefer_1318.
GeneID8366021.
KEGGmfe:Mefer_1318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.

Enzyme and pathway databases

BioCycMFER573064:GHUI-1360-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 nameC7P995_METFA
AccessionPrimary (citable) accession number: C7P995
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: June 11, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)