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Q3SNG2 (RBL1B_NITWN) 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 2

Short name=RuBisCO large subunit 2
EC=4.1.1.39
Gene names
Name:cbbL2
Ordered Locus Names:Nwi_2929
OrganismNitrobacter winogradskyi (strain Nb-255 / ATCC 25391) [Complete proteome] [HAMAP]
Taxonomic identifier323098 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

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 2 HAMAP-Rule MF_01338
PRO_0000251452

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
Q3SNG2 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: E7A0458BCD485A9E

FASTA48954,148
        10         20         30         40         50         60 
MNVQNEKSMT VRGKDRYKSG VMSYKKMGYW EPDYTPKDTD VICLFRVTPQ DGVDPIEASA 

        70         80         90        100        110        120 
AVAGESSTAT WTVVWTDRLT AAEKYRAKCY RVDPVPGAEG QYFAYIAYDL DLFEPGSISN 

       130        140        150        160        170        180 
LTASVIGNVF GFKPLKALRL EDMRLPVAYV KTFKGPPTGI VVERERLDKF GRPLLGATVK 

       190        200        210        220        230        240 
PKLGLSGRNY GRVVYEALKG GLDFTKDDEN INSQPFMHWR ERFLYCMEAV NRAQAATGEI 

       250        260        270        280        290        300 
KGSYLNVTAA TMEDMYERAE FAKELGSVVV MIDLVIGYTA IQSMSNWARK NDMILHLHRA 

       310        320        330        340        350        360 
GHSTYTRQRS HGVSFRVISK WMRLAGVDHI HAGTVVGKLE GDPLTTRGFY DICREEYNPT 

       370        380        390        400        410        420 
QLEHGIFFDQ NWASLNKVMP VASGGIHAGQ MHQLIQHLGE DVVLQFGGGT IGHPMGIQAG 

       430        440        450        460        470        480 
ATANRVALEA MILARNEGRD YVSEGPEILA KAAASCTPLK QALEVWKDVT FDYASTDAPD 


YVPTAVPAA 

« Hide

References

[1]"Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nb-255 / ATCC 25391.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000115 Genomic DNA. Translation: ABA06179.1.
RefSeqYP_319531.1. NC_007406.1.

3D structure databases

ProteinModelPortalQ3SNG2.
SMRQ3SNG2. Positions 26-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323098.Nwi_2929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA06179; ABA06179; Nwi_2929.
GeneID3674284.
KEGGnwi:Nwi_2929.
PATRIC22702997. VBINitWin102302_3305.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMACTPLKQA.
OrthoDBEOG6ZKXMS.

Enzyme and pathway databases

BioCycNWIN323098:GJEG-2980-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 nameRBL1B_NITWN
AccessionPrimary (citable) accession number: Q3SNG2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 11, 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