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UniProtKB/Swiss-Prot entry P24671


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

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Entry information
Entry name RBL_ABIMA
Primary accession number P24671
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on March 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 [Precursor]
Synonyms RuBisCO large subunit
EC 4.1.1.39
Gene name
Name: rbcL
From
Abies magnifica (Red fir) [TaxID: 3320] 
Encoded on Plastid; Chloroplast.
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Coniferopsida; Coniferales; Pinaceae; Abies.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Doerksen A.H., Strauss S., Price R.;
Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
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
X58391; CAA41280.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S14869; RKKHLR.
3D structure databases
HSSP P00880; 1RBL. [HSSP ENTRY / PDB]
SMR P24671; 11-475.
ModBase P24671.
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 P24671.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
PROPEP   1     2  2     By similarity. PRO_0000031099
CHAIN   3   475  473     Ribulose bisphosphate carboxylase large chain. PRO_0000031100
ACT_SITE   175   175        Proton acceptor (By similarity). 
ACT_SITE   294   294        Proton acceptor (By similarity). 
METAL   201   201        Magnesium; via carbamate group (By similarity). 
METAL   203   203        Magnesium (By similarity). 
METAL   204   204        Magnesium (By similarity). 
BINDING   123   123        Substrate; in homodimeric partner (By similarity). 
BINDING   173   173        Substrate (By similarity). 
BINDING   177   177        Substrate (By similarity). 
BINDING   295   295        Substrate (By similarity). 
BINDING   327   327        Substrate (By similarity). 
BINDING   379   379        Substrate (By similarity). 
SITE   334   334  1     Transition state stabilizer (By similarity). 
MOD_RES   3     3        N-acetylproline (By similarity). 
MOD_RES   14    14        N6,N6,N6-trimethyllysine (By similarity). 
MOD_RES   201   201        N6-carboxylysine (By similarity). 
DISULFID   247   247        Interchain; in linked form (By similarity). 
Sequence information
Length: 475 AA [This is the length of the unprocessed precursor] Molecular weight: 52724 Da [This is the MW of the unprocessed precursor] CRC64: 9B701F1839F553EC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSPKTETKAS VGFKAGVKDY RLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV PGEESQFIAY VAYPLDLFEE GSVTNLFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEALYKAQA ETGEIKGHYL 

       250        260        270        280        290        300 
NATAGTCEEM MKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQRNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERD VTLGFVDLLR DDFIEKDRSR 

       370        380        390        400        410        420 
GIFFTQDWVS MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAAAN 

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNEVIREATK WSPELAAACE VWKEIKFEFD TIDYL 

P24671 in FASTA format

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