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UniProtKB/Swiss-Prot entry A5EQ63


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

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Entry information
Entry name RBL1C_BRASB
Primary accession number A5EQ63
Secondary accession numbers None
Integrated into Swiss-Prot on September 11, 2007
Sequence was last modified on June 12, 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 3
Synonyms RuBisCO large subunit 3
EC 4.1.1.39
Gene name
Name: cbbL3
OrderedLocusNames: BBta_6397
From
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [TaxID: 288000] [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
CP000494; ABQ38307.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001242213.1; -.
3D structure databases
ModBase A5EQ63.
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 5154107; -.
GenomeReviews CP000494_GR; BBta_6397.
KEGG bbt:BBta_6397; -.
CMR A5EQ63; BBta_6397.
Other
ProtoNet A5EQ63.
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   486  486     Ribulose bisphosphate carboxylase large chain 3. PRO_0000299960
ACT_SITE   177   177        Proton acceptor (By similarity). 
ACT_SITE   295   295        Proton acceptor (By similarity). 
METAL   203   203        Magnesium; via carbamate group (By similarity). 
METAL   205   205        Magnesium (By similarity). 
METAL   206   206        Magnesium (By similarity). 
BINDING   125   125        Substrate; in homodimeric partner (By similarity). 
BINDING   175   175        Substrate (By similarity). 
BINDING   179   179        Substrate (By similarity). 
BINDING   296   296        Substrate (By similarity). 
BINDING   328   328        Substrate (By similarity). 
BINDING   380   380        Substrate (By similarity). 
SITE   335   335  1     Transition state stabilizer (By similarity). 
MOD_RES   203   203        N6-carboxylysine (By similarity). 
Sequence information
Length: 486 AA [This is the length of the unprocessed precursor] Molecular weight: 53975 Da [This is the MW of the unprocessed precursor] CRC64: A62AC32F3DC5ABF7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNDQSITVRG KDRYKSGVME YKKMGYWEPS YQPKDTDVIA LFRVTPQDGV DPVEACAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTAAE KYRAKCYRVE PVPGSPGSYF AYIAYDLDLF EPGSIANLTA 

       130        140        150        160        170        180 
SIIGNVFGFK PLKALRLEDM RLPVAYVKTF QGPATGIVVE RERLDKFGRP LLGATVKPKL 

       190        200        210        220        230        240 
GLSGRNYGRV VYEALKGGLD FTKDDENINS QPFMHWRERF LYCMEAVNKA QAATGEIKGT 

       250        260        270        280        290        300 
YLNVTAATME DMYERAEFAK ELGSTIIMID LVIGYTAIQS MAKWARRNDM ILHLHRAGHS 

       310        320        330        340        350        360 
TYTRQRAHGV SFRVIAKWMR LAGVDHIHAG TVVGKLEGDP NTTRGYYDIC REDFNPMRLE 

       370        380        390        400        410        420 
HGVFFDQHWA SLNKLMPVAS GGIHAGQMHQ LLDLLGEDVV LQFGGGTIGH PRGIAAGATA 

       430        440        450        460        470        480 
NRVALEAMIL ARNEGRDYVH EGPEILAKAA QTCTPLREAL EIWKDVTFNY ESTDSPDFVP 


TVTPAA 

A5EQ63 in FASTA format

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