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Q2YB78 (RBL_NITMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:Nmul_A0686
OrganismNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849) [Complete proteome] [HAMAP]
Taxonomic identifier323848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira

Protein attributes

Sequence length489 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 – 489489Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000251449

Sites

Active site1801Proton acceptor By similarity
Active site2981Proton acceptor By similarity
Metal binding2061Magnesium; via carbamate group By similarity
Metal binding2081Magnesium By similarity
Metal binding2091Magnesium By similarity
Binding site1281Substrate; in homodimeric partner By similarity
Binding site1781Substrate By similarity
Binding site1821Substrate By similarity
Binding site2991Substrate By similarity
Binding site3311Substrate By similarity
Binding site3831Substrate By similarity
Site3381Transition state stabilizer By similarity

Amino acid modifications

Modified residue2061N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YB78 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 02CFEB7C9D0C2523

FASTA48954,315
        10         20         30         40         50         60 
MSEAITGAER YKSGVIPYKK MGYWEPDYVP KDTDIIAMFR ITPQAGVEPE EAAAAVAGES 

        70         80         90        100        110        120 
STATWTVVWT DRLTACELYR AKAFRTDPVP NTGEGTKTEQ QYFAYIAYDL DLFEPGSIAN 

       130        140        150        160        170        180 
LTASIIGNVF GFKAVKALRL EDMRIPVAYL KTFQGPATGI IVERERLDKF GRPLLGATTK 

       190        200        210        220        230        240 
PKLGLSGRNY GRVVYEGLKG GLDFMKDDEN INSQPFMHWR DRFLYCMEAV NKASAATGEV 

       250        260        270        280        290        300 
KGHYLNVTAG TMEEMYERAE FAKSLGSVII MIDLVIGYTA IQSMAKWARK NDMILHLHRA 

       310        320        330        340        350        360 
GNSTYSRQKN HGMNFRVICK WMRMAGVDHI HAGTVVGKLE GDPLMIKGFY DTLRDRHTPV 

       370        380        390        400        410        420 
SLEHGLFFEQ DWASLNKVMP VASGGIHAGQ MHQLLDYLGE DVILQFGGGT IGHPQGIQAG 

       430        440        450        460        470        480 
AVANRVALEA MIMARNEGRD YVKEGPQILE EAAKWCTPLK LALDTWKDIT FNYESTDTAD 


FVPSETASV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC 25196."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25196 / NCIMB 11849.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000103 Genomic DNA. Translation: ABB73993.1.
RefSeqYP_411385.1. NC_007614.1.

3D structure databases

ProteinModelPortalQ2YB78.
SMRQ2YB78. Positions 10-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323848.Nmul_A0686.

Proteomic databases

PRIDEQ2YB78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB73993; ABB73993; Nmul_A0686.
GeneID3784063.
KEGGnmu:Nmul_A0686.
PATRIC22724432. VBINitMul110821_0791.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycNMUL323848:GKEC-703-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. 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.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL_NITMU
AccessionPrimary (citable) accession number: Q2YB78
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 55 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