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G0JPS3 (G0JPS3_9GAMM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 12. 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 namesRecommended name:
Ribulose bisphosphate carboxylase HAMAP-Rule MF_01339
Short name=RuBisCO HAMAP-Rule MF_01339
EC=4.1.1.39 HAMAP-Rule MF_01339
Gene names
Name:cbbM HAMAP-Rule MF_01339
ORF Names:Acife_1242 EMBL AEM47398.1
OrganismAcidithiobacillus ferrivorans SS3 EMBL AEM47398.1
Taxonomic identifier743299 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus ›

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity. HAMAP-Rule MF_01339

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01339

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01339

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01339

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01339

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity. HAMAP-Rule MF_01339

Sequence similarities

Belongs to the RuBisCO large chain family. Type II subfamily. HAMAP-Rule MF_01339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1661Proton acceptor By similarity HAMAP-Rule MF_01339
Active site2871Proton acceptor By similarity HAMAP-Rule MF_01339
Metal binding1911Magnesium; via carbamate group By similarity HAMAP-Rule MF_01339
Metal binding1931Magnesium By similarity HAMAP-Rule MF_01339
Metal binding1941Magnesium By similarity HAMAP-Rule MF_01339
Binding site1111Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01339
Binding site1681Substrate By similarity HAMAP-Rule MF_01339
Binding site2881Substrate By similarity HAMAP-Rule MF_01339
Binding site3211Substrate By similarity HAMAP-Rule MF_01339
Binding site3681Substrate By similarity HAMAP-Rule MF_01339
Site3291Transition state stabilizer By similarity HAMAP-Rule MF_01339

Amino acid modifications

Modified residue1911N6-carboxylysine By similarity HAMAP-Rule MF_01339

Sequences

Sequence LengthMass (Da)Tools
G0JPS3 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 01DA54B22D6CD319

FASTA45950,246
        10         20         30         40         50         60 
MDQSNRYADL SLRENDLISN GKHILVAYKM KPKAGHGYLE AAAHFAAESS TGTNVEVSTT 

        70         80         90        100        110        120 
DDFTKGVDAL VYHIDEAADD MRIAYPLELF DRNVTDGRMM IVSFLTLVIG NNQGMGDIEH 

       130        140        150        160        170        180 
GQMIDFFMPP RAIQLFDGPA KDISDLWRIL GRPVQNGGYI AGTIIKPKLG LRPEPFAAAA 

       190        200        210        220        230        240 
YQFWLGGDFI KNDEPQGNQV FAPVKKTIPL VYDAMKRAMD ETGAAKLFSM NITADDHYEM 

       250        260        270        280        290        300 
CARADFALET FGPDADKLAF LVDGFVGGPG MITTARRQYP GQYLHYHRAG HGMITSPSAN 

       310        320        330        340        350        360 
RGYTAFVLAK MARLQGASGI HVGTMGYGKM EGGADDRNIA YMIERDSCDG PVYHQEWYGM 

       370        380        390        400        410        420 
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TAGGGAYGHI DSPAAGAVSL RQAYECWKAG 

       430        440        450 
ADPIAYAREH QEFARAFESF PGDADKLYPG WREKLGVHK

« Hide

References

[1]"Draft Genome of the Psychrotolerant Acidophile Acidithiobacillus ferrivorans SS3."
Liljeqvist M., Valdes J., Holmes D.S., Dopson M.
J. Bacteriol. 193:4304-4305(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: SS3 EMBL AEM47398.1.
[2]US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Liljeqvist M. expand/collapse author list , Valdes J., Holmes D., Dopson M., Woyke T.
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: SS3 EMBL AEM47398.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002985 Genomic DNA. Translation: AEM47398.1.
RefSeqYP_004783724.1. NC_015942.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEM47398; AEM47398; Acife_1242.
GeneID11044196.
KEGGafi:Acife_1242.

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycAFER743299:GH39-1254-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01339. RuBisCO_L_type2.
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG0JPS3_9GAMM
AccessionPrimary (citable) accession number: G0JPS3
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: May 1, 2013
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info