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F8GEW5 (F8GEW5_NITSI) 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
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:Nit79A3_1255 EMBL AEJ01097.1
OrganismNitrosomonas sp. (strain Is79A3) [Complete proteome] [HAMAP] EMBL AEJ01097.1
Taxonomic identifier261292 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length473 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_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity. HAMAP-Rule MF_01338

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity. HAMAP-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1681Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2871Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1941Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1971Magnesium By similarity HAMAP-Rule MF_01338
Binding site1161Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1661Substrate By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site2881Substrate By similarity HAMAP-Rule MF_01338
Binding site3201Substrate By similarity HAMAP-Rule MF_01338
Binding site3721Substrate By similarity HAMAP-Rule MF_01338
Site3271Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F8GEW5 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 23F07A35161E6884

FASTA47352,459
        10         20         30         40         50         60 
MAVKIYNAGV KEYRHTYWTP DYTPLDTDLL ACFKITPQAG VPREEVAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYKI EDVPGDDTCF YAFVAYPIDL FEEGSVVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KALRALRLED VRFPIAYVKT CGGPPAGIQV ERDRLNKYGR ALLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DLTKDDENVN SQPFMRWRDR FEFVVEACQK AERETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEFA KELGAPIIMH DYLTGGLTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH 

       310        320        330        340        350        360 
GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DRAATLGWID TMRDKFIKED RSRGLFFDQD 

       370        380        390        400        410        420 
WGSMPGVFPV ASGGIHVWHM PALVAIFGDD ACLQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VEARNQGVEI EKEGKAILTK AAKSSPELKI AMETWKEIKF EFDTVDKLDV AHK 

« Hide

References

[1]"Complete sequence of Nitrosomonas sp. Is79A3."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A. expand/collapse author list , Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.
Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Is79A3 EMBL AEJ01097.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002876 Genomic DNA. Translation: AEJ01097.1.
RefSeqYP_004694496.1. NC_015731.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEJ01097; AEJ01097; Nit79A3_1255.
GeneID10933345.
KEGGnii:Nit79A3_1255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycNSP261292:GH7H-1274-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020888. RuBisCO_lsu.
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.
ProtoNetSearch...

Entry information

Entry nameF8GEW5_NITSI
AccessionPrimary (citable) accession number: F8GEW5
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 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)