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UniProtKB/Swiss-Prot entry A2SJJ7

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

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Entry information
Entry name RBL1B_METPP
Primary accession number A2SJJ7
Secondary accession numbers None
Integrated into Swiss-Prot on September 11, 2007
Sequence was last modified on September 11, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 19)
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: Mpe_A2782
From
Methylibium petroleiphilum (strain PM1) [TaxID: 420662] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01259-06; PubMed=17158667 [NCBI, ExPASy, EBI, Israel, Japan]
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.;
"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1.";
J. Bacteriol. 189:1931-1945(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
CP000555; ABM95736.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001021971.1; -.
3D structure databases
SMR A2SJJ7; 49-515.
ModBase A2SJJ7.
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.
ProtoNet A2SJJ7.
Genome annotation databases
GeneID 4785032; -.
GenomeReviews CP000555_GR; Mpe_A2782.
KEGG mpt:Mpe_A2782; -.
NMPDR fig|279263.3.peg.3495; -.
CMR A2SJJ7; Mpe_A2782.
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; Photosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   485  485     Ribulose bisphosphate carboxylase large chain 2. PRO_0000299965
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: 485 AA [This is the length of the unprocessed precursor] Molecular weight: 53310 Da [This is the MW of the unprocessed precursor] CRC64: 3B36C71F79F2FCAD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNEPTQITDT KKRYAAGVLK YAQMGYWNGD YVPKDTDILA LFRITPQDGV DPIEAAAAVA 

        70         80         90        100        110        120 
GESSTATWTV VWTDRLTACD MYRAKAYKVE PVPNNPGQYF CYVAYDLSLF EEGSIANVTA 

       130        140        150        160        170        180 
SIIGNVFSFK PLKAARLEDM KFPVSYVKTF AGPPTGIVVE RERLDKFGRP LLGATTKPKL 

       190        200        210        220        230        240 
GLSGRNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LFVMDAVNKA SAATGEVKGS 

       250        260        270        280        290        300 
YLNVTAGTME EMYRRAEFAK ELGSVIIMID LVVGYTAIQS MSNWARQNDM VLHMHRAGHG 

       310        320        330        340        350        360 
TYTRQKNHGV SFRVIAKWLR MAGVDHLHTG TAVGKLEGDP LTVQGYYNVC RDTHTKVDLP 

       370        380        390        400        410        420 
RGIFFDQDWG ALKKVMPVAS GGIHAGQMHQ LIDLFGDDVV LQFGGGTIGH PQGIQAGATA 

       430        440        450        460        470        480 
NRVALEAMVL ARNEGRDIKN EGPQILRDAA KSCTPLAAAL DTWGDITFNY TSTDTSDYVP 


TPSVA
A2SJJ7 in FASTA format

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