Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0AHW1 (RBL_NITEC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Ordered Locus Names:Neut_0804
OrganismNitrosomonas eutropha (strain C91) [Complete proteome] [HAMAP]
Taxonomic identifier335283 [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.

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.

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000299966

Sites

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

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AHW1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 0E1D9FEAF68426BC

FASTA47352,688
        10         20         30         40         50         60 
MAIKTYQAGV KEYRQTYWQP DYVPLDTDIL ACFKITPQSG VDREEAAAAV AAESSCGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYRI EDVPGDDARF YAFVAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAIRALRLED VRFPIAYVKT CGGPPSGIQV ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGSL DFTKDDENIN SQPFMRWRDR FEFVQEATLK AEAETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEFA KEIGAPIIMH DYLAGGLCAN AGLANWCRNN GMLLHVHRAM HAVLDRNPHH 

       310        320        330        340        350        360 
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFVPED RSRGIFFDQD 

       370        380        390        400        410        420 
WGSMPGAFAV ASGGIHVWHM PALVAIFGDD SVLQFGGGTL GHPWGNAAGA HANRVALEAC 

       430        440        450        460        470 
VQARNEGRQI EKEGREILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDI AHK 

« Hide

References

[1]"Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C91.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000450 Genomic DNA. Translation: ABI59071.1.
RefSeqYP_747036.1. NC_008344.1.

3D structure databases

ProteinModelPortalQ0AHW1.
SMRQ0AHW1. Positions 16-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335283.Neut_0804.

Proteomic databases

PRIDEQ0AHW1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI59071; ABI59071; Neut_0804.
GeneID4272958.
KEGGnet:Neut_0804.
PATRIC22718721. VBINitEut7577_1030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAMETWKEV.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycNEUT335283:GHT6-821-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 nameRBL_NITEC
AccessionPrimary (citable) accession number: Q0AHW1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families