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UniProtKB/Swiss-Prot entry Q3SNG2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RBL1B_NITWN
Primary accession number Q3SNG2
Secondary accession numbers None
Integrated into Swiss-Prot on October 3, 2006
Sequence was last modified on October 11, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 24)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain 2
Synonyms RuBisCO large subunit 2
EC 4.1.1.39
Gene name
Name: cbbL2
OrderedLocusNames: Nwi_2929
From
Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391) [TaxID: 323098] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Nitrobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/AEM.72.3.2050-2063.2006; PubMed=16517654 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255.";
Appl. Environ. Microbiol. 72:2050-2063(2006).
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).
  • CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
  • CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.
  • COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
  • SUBUNIT: 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).
  • SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000115; ABA06179.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_319531.1; -.
3D structure databases
SMR Q3SNG2; 16-482.
ModBase Q3SNG2.
Enzyme and pathway databases
BioCyc NWIN323098:NWI_2929-MON; -.
Ontologies
GO
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004497; Molecular function: monooxygenase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0016984; Molecular function: ribulose-bisphosphate carboxylase activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019253; Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01338; -; 1.
PBIL [Tree]
InterPro IPR000685; RuBisCO_lsu_C.
IPR017443; RuBisCO_lsu_fd_N.
IPR017444; RuBisCO_lsu_N.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.110; RuBisCO_large; 1.
G3DSA:3.30.70.150; RuBisCO_large; 1.
Pfam PF00016; RuBisCO_large; 1.
PF02788; RuBisCO_large_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00157; RUBISCO_LARGE; 1.
BLOCKS Q3SNG2.
ProtoNet Q3SNG2.
Genome annotation databases
GeneID 3674284; -.
GenomeReviews CP000115_GR; Nwi_2929.
KEGG nwi:Nwi_2929; -.
NMPDR fig|323098.3.peg.2732; -.
Phylogenomic databases
HOGENOM Q3SNG2; -.
Genome annotation databases
CMR Q3SNG2; Nwi_2929.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calvin cycle; Carbon dioxide fixation; Complete proteome; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   489  489     Ribulose bisphosphate carboxylase large chain 2. PRO_0000251452
ACT_SITE   180   180        Proton acceptor (By similarity). 
ACT_SITE   298   298        Proton acceptor (By similarity). 
METAL   206   206        Magnesium; via carbamate group (By similarity). 
METAL   208   208        Magnesium (By similarity). 
METAL   209   209        Magnesium (By similarity). 
BINDING   128   128        Substrate; in homodimeric partner (By similarity). 
BINDING   178   178        Substrate (By similarity). 
BINDING   182   182        Substrate (By similarity). 
BINDING   299   299        Substrate (By similarity). 
BINDING   331   331        Substrate (By similarity). 
BINDING   383   383        Substrate (By similarity). 
SITE   338   338  1     Transition state stabilizer (By similarity). 
MOD_RES   206   206        N6-carboxylysine (By similarity). 
Sequence information
Length: 489 AA [This is the length of the unprocessed precursor] Molecular weight: 54148 Da [This is the MW of the unprocessed precursor] CRC64: E7A0458BCD485A9E [This is a checksum on the sequence] 
        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
Q3SNG2 in FASTA format

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