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UniProtKB/Swiss-Prot entry A4YQD3


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

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Entry information
Entry name RBL1B_BRASO
Primary accession number A4YQD3
Secondary accession numbers None
Integrated into Swiss-Prot on September 11, 2007
Sequence was last modified on May 29, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 13)
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: BRADO2274
From
Bradyrhizobium sp. (strain ORS278) [TaxID: 114615] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Bradyrhizobium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1139548; PubMed=17540897 [NCBI, ExPASy, EBI, Israel, Japan]
Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C., Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
"Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
Science 316:1307-1312(2007).
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
CU234118; CAL76109.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001204346.1; -.
3D structure databases
ModBase A4YQD3.
Ontologies
GO
GO:0009573; Cellular component: chloroplast ribulose bisphosphate carboxylase complex (inferred from electronic annotation from InterPro).
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.
Genome annotation databases
GeneID 5115889; -.
GenomeReviews CU234118_GR; BRADO2274.
KEGG bra:BRADO2274; -.
CMR A4YQD3; BRADO2274.
Other
ProtoNet A4YQD3.
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; Photosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   479  479     Ribulose bisphosphate carboxylase large chain 2. PRO_0000299962
ACT_SITE   168   168        Proton acceptor (By similarity). 
ACT_SITE   287   287        Proton acceptor (By similarity). 
METAL   194   194        Magnesium; via carbamate group (By similarity). 
METAL   196   196        Magnesium (By similarity). 
METAL   197   197        Magnesium (By similarity). 
BINDING   116   116        Substrate; in homodimeric partner (By similarity). 
BINDING   166   166        Substrate (By similarity). 
BINDING   170   170        Substrate (By similarity). 
BINDING   288   288        Substrate (By similarity). 
BINDING   320   320        Substrate (By similarity). 
BINDING   372   372        Substrate (By similarity). 
SITE   327   327  1     Transition state stabilizer (By similarity). 
MOD_RES   194   194        N6-carboxylysine (By similarity). 
Sequence information
Length: 479 AA [This is the length of the unprocessed precursor] Molecular weight: 53334 Da [This is the MW of the unprocessed precursor] CRC64: 7518D7CC0AE30D6C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEKSYQAGV KEYRKTYWTP EYVPLDTDLL AVFKIVAQAG VPREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYRI EPVPGDDNAF YAFIAYPIDL FEEGSVVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRSLRLED IRFPLAYVKT CGGPPNGIQL ERDRLNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENIN SQPFMRWQHR FEFVMEAVHK ATSETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEFA KSLGAPIIMH DFLTAGFTAN TGLANWCREN GMLLHIHRAM HAVLDRNPMH 

       310        320        330        340        350        360 
GIHFRVLTKC LRLSGGDHLH SGTVVGKLEG DREATIGWVD LMREPFVPEN RARGIFFDQD 

       370        380        390        400        410        420 
WGAMPGVMPV ASGGIHVWHM PALTAIFGDD ACFQFGGGTL GHPWGNAAGA HANRVALEAC 

       430        440        450        460        470 
VEARNQGRPV EREGREILTE AAQHSPELKI AMETWKEIKF EFDVVDKLDT GPMLRVVNA 

A4YQD3 in FASTA format

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