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UniProtKB/Swiss-Prot entry P25413


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

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Entry information
Entry name RBL_AEGCR
Primary accession number P25413
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on May 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Ribulose bisphosphate carboxylase large chain [Fragment]
Synonyms RuBisCO large subunit
EC 4.1.1.39
Gene name
Name: rbcL
From
Aegilops crassa (Persian goatgrass) (Triticum crassum) [TaxID: 4481] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Pooideae; Triticeae; Aegilops.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Seedling;
PubMed=1752425 [NCBI, ExPASy, EBI, Israel, Japan]
Ogihara Y., Terachi T., Sasakuma T.;
"Molecular analysis of the hot spot region related to length mutations in wheat chloroplast DNAs. I. Nucleotide divergence of genes and intergenic spacer regions located in the hot spot region.";
Genetics 129:873-884(1991).
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.
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
X62118; CAA44032.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S21984; S21984.
3D structure databases
SMR P25413; 6-420.
ModBase P25413.
Organism-specific databases
Gramene P25413; -.
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:0009853; Biological process: photorespiration (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 P25413.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   <1   421  >421     Ribulose bisphosphate carboxylase large chain. PRO_0000062343
ACT_SITE   120   120        Proton acceptor (By similarity). 
ACT_SITE   239   239        Proton acceptor (By similarity). 
METAL   146   146        Magnesium; via carbamate group (By similarity). 
METAL   148   148        Magnesium (By similarity). 
METAL   149   149        Magnesium (By similarity). 
BINDING   68    68        Substrate; in homodimeric partner (By similarity). 
BINDING   118   118        Substrate (By similarity). 
BINDING   122   122        Substrate (By similarity). 
BINDING   240   240        Substrate (By similarity). 
BINDING   272   272        Substrate (By similarity). 
BINDING   324   324        Substrate (By similarity). 
SITE   279   279  1     Transition state stabilizer (By similarity). 
MOD_RES   146   146        N6-carboxylysine (By similarity). 
DISULFID   192   192        Interchain; in linked form (By similarity). 
NON_TER   1     1         
Sequence information
Length: 421 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 46901 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: 7D247DEFE169CE80 [This is a checksum on the sequence]
        10         20         30         40         50         60 
AVAAESSTGT WTTVWTDGLT SLDRYKGRCY HIEPVAGEDN QWICYVAYPL DLFEEGSVTN 

        70         80         90        100        110        120 
MFTSIVGNVF GFKALRALRL EDLRIPPTYS KTFQGPPHGI QVERDKLNKY GRPLLGCTIK 

       130        140        150        160        170        180 
PKLGLSAKNY GRACYECLRG GLDFTKDDEN VNSQPFMRWR DRFVFCAEAI YKSQAETGEI 

       190        200        210        220        230        240 
KGHYLNATAG TCEEMIKRAV FARELGVPIV MHDYLTGGFT ANTTLRHYCR DNGLLLHIHR 

       250        260        270        280        290        300 
AMHAVIDRQK NHGMHFRVLA KALRMSGGDH IHSGTVVGKL EGEREMTLGF VDLLRDDFIE 

       310        320        330        340        350        360 
KDRARGIFFT QDWVSMPGVI PVASGGIHVW HMPALTEIFG DDSVLQFGGG TLGHPWGNAP 

       370        380        390        400        410        420 
GAAANRVALE ACVQARNEGR DLAREGNEII RAACKWSPEL AAACEVWKAI KFEFEPVDTI 


D 

P25413 in FASTA format

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