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G2TF86 (G2TF86_RHORU) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 17. 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_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:F11_12335 EMBL AEO48931.1
OrganismRhodospirillum rubrum F11 [Complete proteome] EMBL AEO48931.1
Taxonomic identifier1036743 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length466 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
G2TF86 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: 4D9F800450AB0155

FASTA46650,482
        10         20         30         40         50         60 
MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS TGTNVEVCTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEVDEAREL TKIAYPVALF DRNITDGKAM IASFLTLTMG NNQGMGDVEY 

       130        140        150        160        170        180 
AKMHDFYVPE AYRALFDGPS VNISALWKVL GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC 

       190        200        210        220        230        240 
HAFWLGGDFI KNDEPQGNQP FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI 

       250        260        270        280        290        300 
IARGEYVLET FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK 

       310        320        330        340        350        360 
RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG PFYRQSWGGM 

       370        380        390        400        410        420 
KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI DGPVAGARSL RQAWQAWRDG 

       430        440        450        460 
VPVLDYAREH KELARAFESF PGDADQIYPG WRKALGVEDT RSALPA 

« Hide

References

[1]"Identification of a New Gene Required for the Biosynthesis of Rhodoquinone in Rhodospirillum rubrum."
Lonjers Z.T., Dickson E.L., Chu T.P., Kreutz J.E., Neacsu F.A., Anders K.R., Shepherd J.N.
J. Bacteriol. 194:965-971(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: F11 EMBL AEO48931.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003046 Genomic DNA. Translation: AEO48931.1.
RefSeqYP_006048728.1. NC_017584.1.

3D structure databases

ProteinModelPortalG2TF86.
SMRG2TF86. Positions 2-460.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEO48931; AEO48931; F11_12335.
GeneID12643578.
KEGGrrf:F11_12335.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycRRUB1036743:GLJ7-2504-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. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG2TF86_RHORU
AccessionPrimary (citable) accession number: G2TF86
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: February 19, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)