※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||||||
Theoretical PI | 6.22 | ||||||||||||||||||||||||||||||||||
Molecular Weight | 52733 | ||||||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||||||
Protein Name | Ribulose bisphosphate carboxylase large chain; RuBisCO large subunit | ||||||||||||||||||||||||||||||||||
Gene Name | rbcL | ||||||||||||||||||||||||||||||||||
Created Date | 2008-12-16 | ||||||||||||||||||||||||||||||||||
Organism | Brachypodium distachyon(Purple false brome Trachynia distachya) | ||||||||||||||||||||||||||||||||||
NCBI Taxa ID | 15368 | ||||||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description 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). Sequence Annotation propeptide 1 2 chain 3 476 Ribulose bisphosphate carboxylase large chain active site 175 Proton acceptor active site 294 Proton acceptor metal ion-binding site 201 Magnesium; via carbamate group metal ion-binding site 203 Magnesium metal ion-binding site 204 Magnesium binding site 123 Substrate; in homodimeric partner binding site 173 Substrate binding site 177 Substrate binding site 295 Substrate binding site 327 Substrate binding site 379 Substrate site 334 Transition state stabilizer modified residue 3 N-acetylproline modified residue 14 N6,N6,N6-trimethyllysine modified residue 201 N6-carboxylysine disulfide bond 247 Interchain; in linked form Keyword Acetylation,Calvin cycle,Carbon dioxide fixation,Chloroplast,Complete proteome,Disulfide bond,Lyase,Magnesium,Metal-binding,Methylation,Monooxygenase,Oxidoreductase,Photorespiration,Photosynthesis,Plastid,Reference proteome Sequence Source UniProt Protein Sequence MSPQTETKAS VGFKAGVKDY RLTYYTPEYE TKDTDILAAF RVSPQPGVPP EEAGAAVAAE 60 SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEDSQWICY VAYPLDLFEE GSVTNMFTSI 120 VGNVFGFKAL RALRLEDLRI PPTYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 180 SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIYKSQA ETGEIKGHYL 240 NATAGTCEEM MKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV 300 IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDFIEKDRAR 360 GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAAAN 420 RVALEACVQA RNEGRDLARE GNEIIRAACK WSPELAAACE VWKAIKFEFA PVDTID 476 Gene Ontology GO:0009507; C: chloroplast; IEA: UniProtKB-SubCell GO:0000287; F: magnesium ion binding; IEA: UniProtKB-HAMAP GO:0004497; F: monooxygenase activity; IEA: UniProtKB-KW GO:0016984; F: ribulose-bisphosphate carboxylase activity; IEA: UniProtKB-HAMAP GO:0009853; P: photorespiration; IEA: UniProtKB-KW GO:0019253; P: reductive pentose-phosphate cycle; IEA: UniProtKB-KW Interpro Pfam SMART PROSITE PS00157; RUBISCO_LARGE PRINTS |