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UniProtKB/Swiss-Prot entry P30828


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

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Entry information
Entry name RBL_MAGLA
Primary accession number P30828
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    April 8, 2008 (Entry version 51)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain [Fragment]
Synonyms EC 4.1.1.39
RuBisCO large subunit
Gene name
Name: rbcL
From
Magnolia latahensis [TaxID: 3409] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; magnoliids; Magnoliales; Magnoliaceae; Magnolia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/344656a0; PubMed=2325772 [NCBI, ExPASy, EBI, Israel, Japan]
Golenberg E.M., Giannasi D.E., Clegg M.T., Smiley C.J., Durbin M., Henderson D., Zurawski G.;
"Chloroplast DNA sequence from a miocene Magnolia species.";
Nature 344:656-658(1990).
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 in the photorespiration process. 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; disulfide-linked. The disulfide link is formed within the large subunit homodimers (By similarity).
  • SUBCELLULAR LOCATION: Plastid, chloroplast.
  • PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (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.
  • CAUTION: This sequence originates from a miocene fossil leaf sample.
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
X54344; CAA38232.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
SMR P30828; 1-253.
ModBase P30828.
Ontologies
GO
GO:0016984; Molecular function: ribulose-bisphosphate carboxylase activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01338; -; 1.
InterPro IPR000685; RuBisCO_lsu_C.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.110; RuBisCO_large; 1.
Pfam PF00016; RuBisCO_large; 1.
Pfam graphical view of domain structure.
PROSITE PS00157; RUBISCO_LARGE; 1.
BLOCKS P30828.
Other
ProtoNet P30828.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calvin cycle; Carbon dioxide fixation; Chloroplast; Extinct organism protein; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   <1   >253  >253     Ribulose bisphosphate carboxylase large chain. PRO_0000062529
ACT_SITE   87     87        Proton acceptor (By similarity). 
ACT_SITE   206    206        Proton acceptor (By similarity). 
METAL   113    113        Magnesium (via carbamate group) (By similarity). 
METAL   115    115        Magnesium (By similarity). 
METAL   116    116        Magnesium (By similarity). 
BINDING   35     35        Substrate; in homodimeric partner (By similarity). 
BINDING   85     85        Substrate (By similarity). 
BINDING   89     89        Substrate (By similarity). 
BINDING   207    207        Substrate (By similarity). 
BINDING   239    239        Substrate (By similarity). 
SITE   246    246  1     Transition state stabilizer (By similarity). 
MOD_RES   113    113        N6-carboxylysine (By similarity). 
DISULFID   159    159        Interchain; in linked form (By similarity). 
NON_TER   1      1         
NON_TER   253    253         
Sequence information
Length: 253 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 28360 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: F182B07840842950 [This is a checksum on the sequence]
        10         20         30         40         50         60 
PVAGEENQYI AYVAYPLDLF EEGSVTNMFT SIVGNVFGFK ALRALRLEDL RIPTAYVKTF 

        70         80         90        100        110        120 
QGPPHGIQVE RDKLNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS 

       130        140        150        160        170        180 
QPFMRWRDRF LFCAEALYKA QAETGEIKGH YLNATAGTCE EMMKRAIFAR ELGVPIVMHD 

       190        200        210        220        230        240 
YLTGGFTANT SLAHYCRDNG LLLHIHRAMH AVIDRQKNHG IHFRVLAKAL RMSGGDHIHS 

       250 
GTVVGKLEGE RDI 

P30828 in FASTA format

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