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C7RNN3 (C7RNN3_ACCPU) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 28. 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
Ordered Locus Names:CAP2UW1_0825 EMBL ACV34169.1
OrganismAccumulibacter phosphatis (strain UW-1) [Complete proteome] [HAMAP] EMBL ACV34169.1
Taxonomic identifier522306 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Candidatus Accumulibacter ›

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
C7RNN3 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 50263104D5959E2E

FASTA45950,767
        10         20         30         40         50         60 
MDQSNRYADL SLKEEDLIKG GKHILVAYKM KPKAGYDYLP AAAHFAAESS TGTNVEVCTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYHIDEATEE MRIAYPLDLF DRNVTDGRMM IVSFLTLVIG NNQGMGDIEH 

       130        140        150        160        170        180 
AKIYDFYMPE RAIQLFDGPA KDISDMWRVL GRPVKDGGYI AGTIIKPKLG LRPEPFAKAA 

       190        200        210        220        230        240 
YQFWLGGDFI KNDEPQGNQV FAPMKKVMPL VYDAMKRAQD ETGQAKLFSA NITADDHYEM 

       250        260        270        280        290        300 
CARADYILET FGPDADKVAF LVDGYVGGPG MVTTARRQYP NQYLHYHRAG HGAVTSPSSR 

       310        320        330        340        350        360 
RGYDAYVLAK MSRLQGASGI HVGTMGYGKM EGSADDRAIA YVIERDEYQG PAYYQKWYGM 

       370        380        390        400        410        420 
KPTTPIISGG MNALRLPGFF ANLGHGNVIN TSGGGSYGHI DSPAAGAISL RQAYECWKAG 

       430        440        450 
ADPIAWAREH KEFARAFESF PGDADTLYPG WREKLGVHR

« Hide

References

[1]"Complete sequence of chromosome of Candidatus Accumulibacter phosphatis clade IIA str. UW-1."
US DOE Joint Genome Institute
Martin H.G., Ivanova N., Kunin V., Warnecke F., Barry K., He S., Salamov A., Szeto E., Dalin E., Pangilinan J.L., Lapidus A., Lowry S., Kyrpides N.C., McMahon K.D., Hugenholtz P.
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UW-1 EMBL ACV34169.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001715 Genomic DNA. Translation: ACV34169.1.
RefSeqYP_003166098.1. NC_013194.1.

3D structure databases

ProteinModelPortalC7RNN3.
ModBaseSearch...

Protein-protein interaction databases

STRING522306.CAP2UW1_0825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACV34169; ACV34169; CAP2UW1_0825.
GeneID8402960.
KEGGapp:CAP2UW1_0825.
PATRIC21257670. VBICanAcc132554_1098.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
ProtClustDBPRK13475.

Enzyme and pathway databases

BioCycAPHO522306:GHXL-834-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 nameC7RNN3_ACCPU
AccessionPrimary (citable) accession number: C7RNN3
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: May 1, 2013
This is version 28 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